dbPTM

CALX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CALX_HUMAN
UniProt AC	P27824
Protein Name	Calnexin
Gene Name	CANX
Organism	Homo sapiens (Human).
Sequence Length	592
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I membrane protein . Endoplasmic reticulum . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated form pr
Protein Description	Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse..
Protein Sequence	MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Neddylation	DGHDDDVIDIEDDLD CCCCCCEEECCCCHH	5.93	32015554
29	Ubiquitination	DGHDDDVIDIEDDLD CCCCCCEEECCCCHH	5.93	33845483
32 (in isoform 2)	Phosphorylation	-	41.55	22210691
49	Phosphorylation	VEDSKPDTTAPPSSP HHHCCCCCCCCCCCC	33.13	21406692
49	O-linked_Glycosylation	VEDSKPDTTAPPSSP HHHCCCCCCCCCCCC	33.13	OGP
50	Phosphorylation	EDSKPDTTAPPSSPK HHCCCCCCCCCCCCC	44.54	21406692
50	O-linked_Glycosylation	EDSKPDTTAPPSSPK HHCCCCCCCCCCCCC	44.54	OGP
54	Phosphorylation	PDTTAPPSSPKVTYK CCCCCCCCCCCEEEE	59.21	21406692
55	Phosphorylation	DTTAPPSSPKVTYKA CCCCCCCCCCEEEEC	34.22	21406692
59	O-linked_Glycosylation	PPSSPKVTYKAPVPT CCCCCCEEEECCCCC	25.98	23301498
59	Phosphorylation	PPSSPKVTYKAPVPT CCCCCCEEEECCCCC	25.98	23090842
61	Ubiquitination	SSPKVTYKAPVPTGE CCCCEEEECCCCCCC	36.53	29967540
62	Ubiquitination	SPKVTYKAPVPTGEV CCCEEEECCCCCCCE	10.42	33845483
66	Phosphorylation	TYKAPVPTGEVYFAD EEECCCCCCCEEEEC	46.32	28152594
66	O-linked_Glycosylation	TYKAPVPTGEVYFAD EEECCCCCCCEEEEC	46.32	23301498
70	Phosphorylation	PVPTGEVYFADSFDR CCCCCCEEEECCCCC	6.69	24927040
70	Nitration	PVPTGEVYFADSFDR CCCCCCEEEECCCCC	6.69	-
74	Phosphorylation	GEVYFADSFDRGTLS CCEEEECCCCCCCCH	26.14	28152594
77	Methylation	YFADSFDRGTLSGWI EEECCCCCCCCHHHH	37.68	-
79	Phosphorylation	ADSFDRGTLSGWILS ECCCCCCCCHHHHHH	20.74	22673903
79	O-linked_Glycosylation	ADSFDRGTLSGWILS ECCCCCCCCHHHHHH	20.74	55828933
81	Phosphorylation	SFDRGTLSGWILSKA CCCCCCCHHHHHHHH	31.74	21712546
81	O-linked_Glycosylation	SFDRGTLSGWILSKA CCCCCCCHHHHHHHH	31.74	OGP
85	Ubiquitination	GTLSGWILSKAKKDD CCCHHHHHHHHCCCC	3.28	32015554
86	Phosphorylation	TLSGWILSKAKKDDT CCHHHHHHHHCCCCC	22.79	21712546
87	Ubiquitination	LSGWILSKAKKDDTD CHHHHHHHHCCCCCC	61.86	21906983
87	2-Hydroxyisobutyrylation	LSGWILSKAKKDDTD CHHHHHHHHCCCCCC	61.86	-
91	Ubiquitination	ILSKAKKDDTDDEIA HHHHHCCCCCCCHHH	64.43	33845483
93	Phosphorylation	SKAKKDDTDDEIAKY HHHCCCCCCCHHHHH	56.32	28674419
96	Ubiquitination	KKDDTDDEIAKYDGK CCCCCCCHHHHHCCC	47.89	-
99	Ubiquitination	DTDDEIAKYDGKWEV CCCCHHHHHCCCEEH	49.92	32015554
102	Ubiquitination	DEIAKYDGKWEVEEM CHHHHHCCCEEHHHH	33.61	33845483
103	Acetylation	EIAKYDGKWEVEEMK HHHHHCCCEEHHHHH	36.96	26822725
103	Ubiquitination	EIAKYDGKWEVEEMK HHHHHCCCEEHHHHH	36.96	21906983
110	Ubiquitination	KWEVEEMKESKLPGD CEEHHHHHHCCCCCC	63.21	32015554
110	Acetylation	KWEVEEMKESKLPGD CEEHHHHHHCCCCCC	63.21	26051181
113	Ubiquitination	VEEMKESKLPGDKGL HHHHHHCCCCCCCEE	60.85	23000965
113	2-Hydroxyisobutyrylation	VEEMKESKLPGDKGL HHHHHHCCCCCCCEE	60.85	-
118	Ubiquitination	ESKLPGDKGLVLMSR HCCCCCCCEEEEEEC	61.12	23000965
118	2-Hydroxyisobutyrylation	ESKLPGDKGLVLMSR HCCCCCCCEEEEEEC	61.12	-
118	Acetylation	ESKLPGDKGLVLMSR HCCCCCCCEEEEEEC	61.12	25953088
119	Ubiquitination	SKLPGDKGLVLMSRA CCCCCCCEEEEEECH	26.26	32015554
119	Ubiquitination	SKLPGDKGLVLMSRA CCCCCCCEEEEEECH	26.26	21890473
122	Ubiquitination	PGDKGLVLMSRAKHH CCCCEEEEEECHHHH	2.87	32015554
125	Methylation	KGLVLMSRAKHHAIS CEEEEEECHHHHHHH	33.42	-
125	Ubiquitination	KGLVLMSRAKHHAIS CEEEEEECHHHHHHH	33.42	32142685
127	Ubiquitination	LVLMSRAKHHAISAK EEEEECHHHHHHHHC	34.51	27667366
127	2-Hydroxyisobutyrylation	LVLMSRAKHHAISAK EEEEECHHHHHHHHC	34.51	-
134	Acetylation	KHHAISAKLNKPFLF HHHHHHHCCCCCCCC	45.89	19811587
134	Ubiquitination	KHHAISAKLNKPFLF HHHHHHHCCCCCCCC	45.89	23000965
137	Acetylation	AISAKLNKPFLFDTK HHHHCCCCCCCCCCC	47.81	19608861
137	Ubiquitination	AISAKLNKPFLFDTK HHHHCCCCCCCCCCC	47.81	23000965
137	Neddylation	AISAKLNKPFLFDTK HHHHCCCCCCCCCCC	47.81	32015554
138	Ubiquitination	ISAKLNKPFLFDTKP HHHCCCCCCCCCCCC	30.05	32015554
141	Ubiquitination	KLNKPFLFDTKPLIV CCCCCCCCCCCCEEE	13.18	21890473
145	Ubiquitination	PFLFDTKPLIVQYEV CCCCCCCCEEEEEEE	29.43	32015554
153	Ubiquitination	LIVQYEVNFQNGIEC EEEEEEEECCCCCEE	22.35	32015554
157	Ubiquitination	YEVNFQNGIECGGAY EEEECCCCCEECHHH	13.29	21890473
164	Ubiquitination	GIECGGAYVKLLSKT CCEECHHHHHHHHCC	11.03	32015554
166	Ubiquitination	ECGGAYVKLLSKTPE EECHHHHHHHHCCCC	30.91	23000965
167	Ubiquitination	CGGAYVKLLSKTPEL ECHHHHHHHHCCCCC	4.69	23000965
170	Ubiquitination	AYVKLLSKTPELNLD HHHHHHHCCCCCCHH	68.98	23000965
170	2-Hydroxyisobutyrylation	AYVKLLSKTPELNLD HHHHHHHCCCCCCHH	68.98	-
170	Malonylation	AYVKLLSKTPELNLD HHHHHHHCCCCCCHH	68.98	33225896
170	Acetylation	AYVKLLSKTPELNLD HHHHHHHCCCCCCHH	68.98	25953088
172	Ubiquitination	VKLLSKTPELNLDQF HHHHHCCCCCCHHHH	48.06	21890473
172	Neddylation	VKLLSKTPELNLDQF HHHHHCCCCCCHHHH	48.06	32015554
181	Ubiquitination	LNLDQFHDKTPYTIM CCHHHHCCCCCEEEE	58.79	27667366
182	Ubiquitination	NLDQFHDKTPYTIMF CHHHHCCCCCEEEEE	42.71	21890473
182	2-Hydroxyisobutyrylation	NLDQFHDKTPYTIMF CHHHHCCCCCEEEEE	42.71	-
182	Acetylation	NLDQFHDKTPYTIMF CHHHHCCCCCEEEEE	42.71	26051181
185	Phosphorylation	QFHDKTPYTIMFGPD HHCCCCCEEEEECCC	17.71	-
188	Ubiquitination	DKTPYTIMFGPDKCG CCCCEEEEECCCCCC	2.15	23000965
191	Ubiquitination	PYTIMFGPDKCGEDY CEEEEECCCCCCCCE	26.99	21890473
191	Neddylation	PYTIMFGPDKCGEDY CEEEEECCCCCCCCE	26.99	32015554
193	Ubiquitination	TIMFGPDKCGEDYKL EEEECCCCCCCCEEE	47.47	32015554
193	2-Hydroxyisobutyrylation	TIMFGPDKCGEDYKL EEEECCCCCCCCEEE	47.47	-
193	Acetylation	TIMFGPDKCGEDYKL EEEECCCCCCCCEEE	47.47	27452117
198	Phosphorylation	PDKCGEDYKLHFIFR CCCCCCCEEEEEEEE	15.90	28152594
199	Acetylation	DKCGEDYKLHFIFRH CCCCCCEEEEEEEEC	48.05	155557
199	Ubiquitination	DKCGEDYKLHFIFRH CCCCCCEEEEEEEEC	48.05	33845483
205	Ubiquitination	YKLHFIFRHKNPKTG EEEEEEEECCCCCCC	34.75	33845483
210	Ubiquitination	IFRHKNPKTGIYEEK EEECCCCCCCCCCHH	69.63	27667366
210	2-Hydroxyisobutyrylation	IFRHKNPKTGIYEEK EEECCCCCCCCCCHH	69.63	-
211	Phosphorylation	FRHKNPKTGIYEEKH EECCCCCCCCCCHHH	30.03	28152594
214	Phosphorylation	KNPKTGIYEEKHAKR CCCCCCCCCHHHCCC	21.27	28152594
217	Acetylation	KTGIYEEKHAKRPDA CCCCCCHHHCCCCCC	36.60	25825284
217	Ubiquitination	KTGIYEEKHAKRPDA CCCCCCHHHCCCCCC	36.60	29967540
217	2-Hydroxyisobutyrylation	KTGIYEEKHAKRPDA CCCCCCHHHCCCCCC	36.60	-
220	Ubiquitination	IYEEKHAKRPDADLK CCCHHHCCCCCCCHH	65.27	23000965
224	Ubiquitination	KHAKRPDADLKTYFT HHCCCCCCCHHHHCC	27.07	21890473
227	Acetylation	KRPDADLKTYFTDKK CCCCCCHHHHCCCCC	41.55	25825284
227	Ubiquitination	KRPDADLKTYFTDKK CCCCCCHHHHCCCCC	41.55	21906983
227	2-Hydroxyisobutyrylation	KRPDADLKTYFTDKK CCCCCCHHHHCCCCC	41.55	-
228	Phosphorylation	RPDADLKTYFTDKKT CCCCCHHHHCCCCCC	31.03	28152594
228	Ubiquitination	RPDADLKTYFTDKKT CCCCCHHHHCCCCCC	31.03	32015554
229	Phosphorylation	PDADLKTYFTDKKTH CCCCHHHHCCCCCCE	11.68	28152594
233	Ubiquitination	LKTYFTDKKTHLYTL HHHHCCCCCCEEEEE	57.42	32142685
233	2-Hydroxyisobutyrylation	LKTYFTDKKTHLYTL HHHHCCCCCCEEEEE	57.42	-
233	Acetylation	LKTYFTDKKTHLYTL HHHHCCCCCCEEEEE	57.42	27178108
234	Ubiquitination	KTYFTDKKTHLYTLI HHHCCCCCCEEEEEE	43.94	33845483
234	Ubiquitination	KTYFTDKKTHLYTLI HHHCCCCCCEEEEEE	43.94	-
236	Ubiquitination	YFTDKKTHLYTLILN HCCCCCCEEEEEEEC	26.22	21890473
245	Ubiquitination	YTLILNPDNSFEILV EEEEECCCCCEEEEE	63.43	33845483
247	Ubiquitination	LILNPDNSFEILVDQ EEECCCCCEEEEECH	31.47	32015554
253	Ubiquitination	NSFEILVDQSVVNSG CCEEEEECHHHHCCC	31.43	33845483
262	Ubiquitination	SVVNSGNLLNDMTPP HHHCCCCCCCCCCCC	5.58	32015554
264	Ubiquitination	VNSGNLLNDMTPPVN HCCCCCCCCCCCCCC	39.93	33845483
268	Ubiquitination	NLLNDMTPPVNPSRE CCCCCCCCCCCCCCC	24.97	32142685
268	Ubiquitination	NLLNDMTPPVNPSRE CCCCCCCCCCCCCCC	24.97	-
269	Ubiquitination	LLNDMTPPVNPSREI CCCCCCCCCCCCCCC	29.38	-
272	Ubiquitination	DMTPPVNPSREIEDP CCCCCCCCCCCCCCC	34.69	33845483
281	Ubiquitination	REIEDPEDRKPEDWD CCCCCCCCCCCCCCC	70.10	21890473
282	Methylation	EIEDPEDRKPEDWDE CCCCCCCCCCCCCCC	55.56	-
283	Ubiquitination	IEDPEDRKPEDWDER CCCCCCCCCCCCCCC	66.15	29967540
287	Ubiquitination	EDRKPEDWDERPKIP CCCCCCCCCCCCCCC	14.01	32142685
293	Ubiquitination	DWDERPKIPDPEAVK CCCCCCCCCCHHHCC	5.32	29901268
300	Ubiquitination	IPDPEAVKPDDWDED CCCHHHCCCCCCCCC	50.18	29967540
350	Ubiquitination	DEDMDGEWEAPQIAN CCCCCCCCCCCCCCC	16.75	33845483
362	Phosphorylation	IANPRCESAPGCGVW CCCCCCCCCCCCCCC	43.31	-
379	Phosphorylation	PVIDNPNYKGKWKPP CCCCCCCCCCCCCCC	23.52	-
380	Ubiquitination	VIDNPNYKGKWKPPM CCCCCCCCCCCCCCC	61.73	27667366
380	Acetylation	VIDNPNYKGKWKPPM CCCCCCCCCCCCCCC	61.73	26051181
382	Ubiquitination	DNPNYKGKWKPPMID CCCCCCCCCCCCCCC	48.14	-
392	Phosphorylation	PPMIDNPSYQGIWKP CCCCCCCCCCCCCCC	36.02	20068231
393	Phosphorylation	PMIDNPSYQGIWKPR CCCCCCCCCCCCCCC	16.41	20068231
398	Ubiquitination	PSYQGIWKPRKIPNP CCCCCCCCCCCCCCC	32.78	21890473
398	Ubiquitination	PSYQGIWKPRKIPNP CCCCCCCCCCCCCCC	32.78	21890473
398	Acetylation	PSYQGIWKPRKIPNP CCCCCCCCCCCCCCC	32.78	26051181
401	Ubiquitination	QGIWKPRKIPNPDFF CCCCCCCCCCCCCCC	71.67	22053931
401	2-Hydroxyisobutyrylation	QGIWKPRKIPNPDFF CCCCCCCCCCCCCCC	71.67	-
407	Ubiquitination	RKIPNPDFFEDLEPF CCCCCCCCCCCCCCC	8.34	33845483
408	Ubiquitination	KIPNPDFFEDLEPFR CCCCCCCCCCCCCCC	10.47	33845483
414	Ubiquitination	FFEDLEPFRMTPFSA CCCCCCCCCCCCHHH	6.43	33845483
415	Ubiquitination	FEDLEPFRMTPFSAI CCCCCCCCCCCHHHH	38.49	33845483
415	Ubiquitination	FEDLEPFRMTPFSAI CCCCCCCCCCCHHHH	38.49	-
417	Ubiquitination	DLEPFRMTPFSAIGL CCCCCCCCCHHHHHH	19.54	33845483
417	Ubiquitination	DLEPFRMTPFSAIGL CCCCCCCCCHHHHHH	19.54	-
423	Ubiquitination	MTPFSAIGLELWSMT CCCHHHHHHHHHHHC	16.89	33845483
429	Ubiquitination	IGLELWSMTSDIFFD HHHHHHHHCCCCHHC	2.55	33845483
431	Phosphorylation	LELWSMTSDIFFDNF HHHHHHCCCCHHCCE	21.77	-
434	Ubiquitination	WSMTSDIFFDNFIIC HHHCCCCHHCCEEEE	8.26	21963094
435	Ubiquitination	SMTSDIFFDNFIICA HHCCCCHHCCEEEEE	8.41	29901268
436	Ubiquitination	MTSDIFFDNFIICAD HCCCCHHCCEEEEEC	38.08	29901268
439	Ubiquitination	DIFFDNFIICADRRI CCHHCCEEEEECCCC	2.95	33845483
445	Ubiquitination	FIICADRRIVDDWAN EEEEECCCCCCCCHH	33.55	33845483
446	Phosphorylation	IICADRRIVDDWAND EEEECCCCCCCCHHC	4.08	32142685
452	Ubiquitination	RIVDDWANDGWGLKK CCCCCCHHCCCCCHH	44.04	21890473
455	Ubiquitination	DDWANDGWGLKKAAD CCCHHCCCCCHHHHC	16.29	22053931
456	Phosphorylation	DWANDGWGLKKAADG CCHHCCCCCHHHHCC	32.90	32142685
458	Acetylation	ANDGWGLKKAADGAA HHCCCCCHHHHCCCC	36.11	26822725
458	Ubiquitination	ANDGWGLKKAADGAA HHCCCCCHHHHCCCC	36.11	21906983
458	2-Hydroxyisobutyrylation	ANDGWGLKKAADGAA HHCCCCCHHHHCCCC	36.11	-
459	Acetylation	NDGWGLKKAADGAAE HCCCCCHHHHCCCCC	54.58	156283
459	Ubiquitination	NDGWGLKKAADGAAE HCCCCCHHHHCCCCC	54.58	23503661
463	Ubiquitination	GLKKAADGAAEPGVV CCHHHHCCCCCCCHH	23.20	32142685
475	Phosphorylation	GVVGQMIEAAEERPW CHHHHHHHHHHHCCH	36.16	32142685
492	Ubiquitination	VVYILTVALPVFLVI HHHHHHHHHHHHHHH	10.83	33845483
493	Ubiquitination	VYILTVALPVFLVIL HHHHHHHHHHHHHHH	3.02	33845483
493	Ubiquitination	VYILTVALPVFLVIL HHHHHHHHHHHHHHH	3.02	-
494	Ubiquitination	YILTVALPVFLVILF HHHHHHHHHHHHHHH	12.70	-
502	S-palmitoylation	VFLVILFCCSGKKQT HHHHHHHHCCCCCCC	1.29	22314232
503	S-palmitoylation	FLVILFCCSGKKQTS HHHHHHHCCCCCCCC	4.75	22314232
509	Phosphorylation	CCSGKKQTSGMEYKK HCCCCCCCCCCCCCC	35.81	-
510	Phosphorylation	CSGKKQTSGMEYKKT CCCCCCCCCCCCCCC	33.38	-
512	Ubiquitination	GKKQTSGMEYKKTDA CCCCCCCCCCCCCCC	5.22	21963094
513	Ubiquitination	KKQTSGMEYKKTDAP CCCCCCCCCCCCCCC	58.70	23503661
514	Phosphorylation	KQTSGMEYKKTDAPQ CCCCCCCCCCCCCCC	14.64	-
515	Ubiquitination	QTSGMEYKKTDAPQP CCCCCCCCCCCCCCC	35.57	21906983
515	2-Hydroxyisobutyrylation	QTSGMEYKKTDAPQP CCCCCCCCCCCCCCC	35.57	-
516	Ubiquitination	TSGMEYKKTDAPQPD CCCCCCCCCCCCCCC	51.22	21906983
517	Phosphorylation	SGMEYKKTDAPQPDV CCCCCCCCCCCCCCC	32.99	21601212
523	Ubiquitination	KTDAPQPDVKEEEEE CCCCCCCCCHHHHHH	59.89	33845483
525	Ubiquitination	DAPQPDVKEEEEEKE CCCCCCCHHHHHHHH	67.78	21906983
525	Sumoylation	DAPQPDVKEEEEEKE CCCCCCCHHHHHHHH	67.78	-
529	Ubiquitination	PDVKEEEEEKEEEKD CCCHHHHHHHHHHHH	77.10	33845483
531	Ubiquitination	VKEEEEEKEEEKDKG CHHHHHHHHHHHHCC	73.95	33845483
531	Acetylation	VKEEEEEKEEEKDKG CHHHHHHHHHHHHCC	73.95	23236377
535	Ubiquitination	EEEKEEEKDKGDEEE HHHHHHHHHCCCHHH	68.93	33845483
537	Ubiquitination	EKEEEKDKGDEEEEG HHHHHHHCCCHHHHH	78.36	21906983
545	Ubiquitination	GDEEEEGEEKLEEKQ CCHHHHHHHHHHHHH	56.06	33845483
547	Ubiquitination	EEEEGEEKLEEKQKS HHHHHHHHHHHHHHH	57.82	33845483
549	Ubiquitination	EEGEEKLEEKQKSDA HHHHHHHHHHHHHHC	74.37	33845483
550	Ubiquitination	EGEEKLEEKQKSDAE HHHHHHHHHHHHHCC	71.82	33845483
551	Ubiquitination	GEEKLEEKQKSDAEE HHHHHHHHHHHHCCC	54.36	33845483
551	Ubiquitination	GEEKLEEKQKSDAEE HHHHHHHHHHHHCCC	54.36	-
552	Phosphorylation	EEKLEEKQKSDAEED HHHHHHHHHHHCCCC	54.48	32142685
553	Ubiquitination	EKLEEKQKSDAEEDG HHHHHHHHHHCCCCC	62.46	33845483
554	Phosphorylation	KLEEKQKSDAEEDGG HHHHHHHHHCCCCCC	39.29	29255136
559	Ubiquitination	QKSDAEEDGGTVSQE HHHHCCCCCCCCCHH	52.94	33845483
560	Ubiquitination	KSDAEEDGGTVSQEE HHHCCCCCCCCCHHH	36.63	33845483
560	Ubiquitination	KSDAEEDGGTVSQEE HHHCCCCCCCCCHHH	36.63	-
562	Phosphorylation	DAEEDGGTVSQEEED HCCCCCCCCCHHHHH	23.63	29255136
563	Phosphorylation	AEEDGGTVSQEEEDR CCCCCCCCCHHHHHC	6.68	32142685
564	Phosphorylation	EEDGGTVSQEEEDRK CCCCCCCCHHHHHCC	31.54	29255136
565	Ubiquitination	EDGGTVSQEEEDRKP CCCCCCCHHHHHCCC	58.76	33845483
566	Ubiquitination	DGGTVSQEEEDRKPK CCCCCCHHHHHCCCC	56.71	33845483
566	Acetylation	DGGTVSQEEEDRKPK CCCCCCHHHHHCCCC	56.71	-
569	Ubiquitination	TVSQEEEDRKPKAEE CCCHHHHHCCCCHHH	68.15	21890473
570	Ubiquitination	VSQEEEDRKPKAEED CCHHHHHCCCCHHHH	61.53	33845483
571	Ubiquitination	SQEEEDRKPKAEEDE CHHHHHCCCCHHHHH	64.29	33845483
572	Ubiquitination	QEEEDRKPKAEEDEI HHHHHCCCCHHHHHH	41.82	33845483
572	Ubiquitination	QEEEDRKPKAEEDEI HHHHHCCCCHHHHHH	41.82	-
573	Ubiquitination	EEEDRKPKAEEDEIL HHHHCCCCHHHHHHH	72.04	24816145
579	Ubiquitination	PKAEEDEILNRSPRN CCHHHHHHHHCCCCC	6.81	33845483
581	Ubiquitination	AEEDEILNRSPRNRK HHHHHHHHCCCCCCC	48.31	33845483
581	Phosphorylation	AEEDEILNRSPRNRK HHHHHHHHCCCCCCC	48.31	32142685
582	Ubiquitination	EEDEILNRSPRNRKP HHHHHHHCCCCCCCC	44.59	33845483
582	Phosphorylation	EEDEILNRSPRNRKP HHHHHHHCCCCCCCC	44.59	32142685
582	Ubiquitination	EEDEILNRSPRNRKP HHHHHHHCCCCCCCC	44.59	-
583	Phosphorylation	EDEILNRSPRNRKPR HHHHHHCCCCCCCCC	27.43	25159151
585	Ubiquitination	EILNRSPRNRKPRRE HHHHCCCCCCCCCCC	57.75	33845483
587	Ubiquitination	LNRSPRNRKPRRE-- HHCCCCCCCCCCC--	52.19	33845483
588	Phosphorylation	NRSPRNRKPRRE--- HCCCCCCCCCCC---	46.56	32142685
588	Ubiquitination	NRSPRNRKPRRE--- HCCCCCCCCCCC---	46.56	33845483
589	Phosphorylation	RSPRNRKPRRE---- CCCCCCCCCCC----	37.01	32142685
591	Ubiquitination	PRNRKPRRE------ CCCCCCCCC------	63.60	33845483
598	Phosphorylation	RE------------- CC-------------		32142685
599	Phosphorylation	E-------------- C--------------		32142685
601	Ubiquitination	---------------- ----------------		33845483
605	Ubiquitination	-------------------- --------------------		32142685
606	Ubiquitination	--------------------- ---------------------		32142685
607	Ubiquitination	---------------------- ----------------------		33845483
608	Phosphorylation	----------------------- -----------------------		32142685
617	Phosphorylation	-------------------------------- --------------------------------		32142685
618	Phosphorylation	--------------------------------- ---------------------------------		32142685
625	Ubiquitination	---------------------------------------- ----------------------------------------		32142685
627	Ubiquitination	------------------------------------------ ------------------------------------------		24816145
637	Phosphorylation	---------------------------------------------------- ----------------------------------------------------		32142685

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
554	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
554	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
564	S	Phosphorylation	Kinase	MAPK3	P27361	Uniprot
564	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
564	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
583	S	Phosphorylation	Kinase	CDK1	P06493	PSP
583	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
583	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
583	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
583	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
564	S	Phosphorylation		18669648
Phosphorylated at Ser-564 by MAPK3/ERK1.

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 CALX_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APOB_HUMAN	APOB	physical	14498830
EDEM1_HUMAN	EDEM1	physical	12610305
TRFE_HUMAN	TF	physical	9312001
TSHR_HUMAN	TSHR	physical	12383251
ZNRF4_HUMAN	ZNRF4	physical	21205830
EDEM1_MOUSE	Edem1	physical	22905195
ACHA5_HUMAN	CHRNA5	physical	9642271
A2AP_HUMAN	SERPINF2	physical	10671537
KCNH2_HUMAN	KCNH2	physical	22242185
GLU2B_HUMAN	PRKCSH	physical	22939629
GANAB_HUMAN	GANAB	physical	22939629
RPN2_HUMAN	RPN2	physical	22939629
ASGR1_HUMAN	ASGR1	physical	23233672
A1AT_HUMAN	SERPINA1	physical	17380188
PDIA3_HUMAN	PDIA3	physical	12052826
NPHN_HUMAN	NPHS1	physical	24303155
MRP1_HUMAN	ABCC1	physical	26344197
MRP3_HUMAN	ABCC3	physical	26344197
AT131_HUMAN	ATP13A1	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26344197
CLH1_HUMAN	CLTC	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
CY1_HUMAN	CYC1	physical	26344197
ETFA_HUMAN	ETFA	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
KDSR_HUMAN	KDSR	physical	26344197
IMA1_HUMAN	KPNA2	physical	26344197
MOGS_HUMAN	MOGS	physical	26344197
COX2_HUMAN	COX2	physical	26344197
NCLN_HUMAN	NCLN	physical	26344197
PYC_HUMAN	PC	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RCN1_HUMAN	RCN1	physical	26344197
RPN2_HUMAN	RPN2	physical	26344197
SPTN1_HUMAN	SPTAN1	physical	26344197
EFTU_HUMAN	TUFM	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
TERA_HUMAN	VCP	physical	26344197
GGT1_HUMAN	GGT1	physical	21712391
BSCL2_HUMAN	BSCL2	physical	17387721

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 CALX_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-137, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-554 AND SER-564, ANDMASS SPECTROMETRY.	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-554; SER-564 ANDSER-583, AND MASS SPECTROMETRY.	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-583, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, ANDMASS SPECTROMETRY.	18318008 [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-554; SER-564 ANDSER-583, 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-554 AND SER-583, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 ANDSER-583, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND MASSSPECTROMETRY.	19007248 [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-583, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562 AND SER-583, ANDMASS SPECTROMETRY.	16565220 [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-554; SER-564 ANDSER-583, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASSSPECTROMETRY.	16083285 [Abstract]

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