dbPTM

CALU_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CALU_HUMAN
UniProt AC	O43852
Protein Name	Calumenin
Gene Name	CALU
Organism	Homo sapiens (Human).
Sequence Length	315
Subcellular Localization	Endoplasmic reticulum membrane . Golgi apparatus . Secreted . Melanosome . Sarcoplasmic reticulum lumen . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity)..
Protein Sequence	MDLRQFLMCLSLCTAFALSKPTEKKDRVHHEPQLSDKVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4 (in isoform 14)	Phosphorylation	-	22.42	24043423
4 (in isoform 3)	Phosphorylation	-	22.42	24043423
4 (in isoform 4)	Phosphorylation	-	22.42	24043423
19 (in isoform 14)	Phosphorylation	-	32.91	24043423
19 (in isoform 3)	Phosphorylation	-	32.91	24043423
19 (in isoform 4)	Phosphorylation	-	32.91	24043423
22 (in isoform 14)	Phosphorylation	-	65.26	24043423
22 (in isoform 3)	Phosphorylation	-	65.26	24043423
22 (in isoform 4)	Phosphorylation	-	65.26	24043423
27 (in isoform 14)	Phosphorylation	-	38.25	24043423
27 (in isoform 3)	Phosphorylation	-	38.25	24043423
27 (in isoform 4)	Phosphorylation	-	38.25	24043423
35	Phosphorylation	VHHEPQLSDKVHNDA CCCCCCHHHHHCCCH	30.09	23927012
35	O-linked_Glycosylation	VHHEPQLSDKVHNDA CCCCCCHHHHHCCCH	30.09	OGP
37	Ubiquitination	HEPQLSDKVHNDAQS CCCCHHHHHCCCHHH	41.85	-
44	Phosphorylation	KVHNDAQSFDYDHDA HHCCCHHHCCCCCHH	23.08	20201521
47	Phosphorylation	NDAQSFDYDHDAFLG CCHHHCCCCCHHCCC	17.11	28355574
59	Ubiquitination	FLGAEEAKTFDQLTP CCCHHHHCCHHHCCH	53.67	-
60	Phosphorylation	LGAEEAKTFDQLTPE CCHHHHCCHHHCCHH	39.22	25159151
60	O-linked_Glycosylation	LGAEEAKTFDQLTPE CCHHHHCCHHHCCHH	39.22	51377199
60 (in isoform 2)	Phosphorylation	-	39.22	25159151
60 (in isoform 7)	Phosphorylation	-	39.22	25159151
60 (in isoform 8)	Phosphorylation	-	39.22	25159151
65	Phosphorylation	AKTFDQLTPEESKER HCCHHHCCHHHHHHH	24.03	25159151
65 (in isoform 2)	Phosphorylation	-	24.03	25159151
65 (in isoform 7)	Phosphorylation	-	24.03	25159151
65 (in isoform 8)	Phosphorylation	-	24.03	25159151
68 (in isoform 4)	Phosphorylation	-	69.21	25159151
69	Phosphorylation	DQLTPEESKERLGKI HHCCHHHHHHHHHHH	37.85	28355574
69 (in isoform 2)	Phosphorylation	-	37.85	25849741
69 (in isoform 7)	Phosphorylation	-	37.85	25849741
69 (in isoform 8)	Phosphorylation	-	37.85	25849741
70	Sumoylation	QLTPEESKERLGKIV HCCHHHHHHHHHHHH	50.57	-
70	Ubiquitination	QLTPEESKERLGKIV HCCHHHHHHHHHHHH	50.57	21906983
70	Sumoylation	QLTPEESKERLGKIV HCCHHHHHHHHHHHH	50.57	-
70 (in isoform 2)	Ubiquitination	-	50.57	21890473
73 (in isoform 15)	Phosphorylation	-	9.57	-
73 (in isoform 4)	Phosphorylation	-	9.57	25159151
75	Ubiquitination	ESKERLGKIVSKIDG HHHHHHHHHHHHHCC	44.52	-
77 (in isoform 4)	Phosphorylation	-	5.63	25849741
78 (in isoform 1)	Ubiquitination	-	27.63	21890473
79	Ubiquitination	RLGKIVSKIDGDKDG HHHHHHHHHCCCCCC	33.64	-
79	Acetylation	RLGKIVSKIDGDKDG HHHHHHHHHCCCCCC	33.64	27452117
84	Ubiquitination	VSKIDGDKDGFVTVD HHHHCCCCCCCEEHH	66.34	21890473
89	Phosphorylation	GDKDGFVTVDELKDW CCCCCCEEHHHHHHH	21.70	-
92	Ubiquitination	DGFVTVDELKDWIKF CCCEEHHHHHHHHHH	54.07	21890473
94	Ubiquitination	FVTVDELKDWIKFAQ CEEHHHHHHHHHHHH	49.31	21890473
94 (in isoform 2)	Ubiquitination	-	49.31	21890473
98	Ubiquitination	DELKDWIKFAQKRWI HHHHHHHHHHHHHHC	30.32	983
98	Acetylation	DELKDWIKFAQKRWI HHHHHHHHHHHHHHC	30.32	27452117
102	Ubiquitination	DWIKFAQKRWIYEDV HHHHHHHHHHCHHCH	46.39	-
102	Ubiquitination	DWIKFAQKRWIYEDV HHHHHHHHHHCHHCH	46.39	21890473
106	Phosphorylation	FAQKRWIYEDVERQW HHHHHHCHHCHHHHH	10.10	25884760
106	Ubiquitination	FAQKRWIYEDVERQW HHHHHHCHHCHHHHH	10.10	21890473
111	Methylation	WIYEDVERQWKGHDL HCHHCHHHHHCCCCC	47.73	-
114	Ubiquitination	EDVERQWKGHDLNED HCHHHHHCCCCCCCC	37.72	21890473
122	Ubiquitination	GHDLNEDGLVSWEEY CCCCCCCCCCCHHHH	23.07	21890473
125	Phosphorylation	LNEDGLVSWEEYKNA CCCCCCCCHHHHCCC	33.54	25159151
129	Phosphorylation	GLVSWEEYKNATYGY CCCCHHHHCCCCEEE	9.68	-
130	Ubiquitination	LVSWEEYKNATYGYV CCCHHHHCCCCEEEE	43.30	-
131	N-linked_Glycosylation	VSWEEYKNATYGYVL CCHHHHCCCCEEEEC	36.29	19139490
150	Ubiquitination	PDDGFNYKQMMVRDE CCCCCCHHHEEHHCH	32.59	-
150 (in isoform 2)	Ubiquitination	-	32.59	-
162	Sulfoxidation	RDERRFKMADKDGDL HCHHHHCCCCCCCCE	5.54	21406390
165	Acetylation	RRFKMADKDGDLIAT HHHCCCCCCCCEEEE	54.81	26051181
165	Ubiquitination	RRFKMADKDGDLIAT HHHCCCCCCCCEEEE	54.81	-
172	Phosphorylation	KDGDLIATKEEFTAF CCCCEEEEHHHHHHH	31.81	29083192
173	Ubiquitination	DGDLIATKEEFTAFL CCCEEEEHHHHHHHC	46.34	-
177	Phosphorylation	IATKEEFTAFLHPEE EEEHHHHHHHCCHHH	21.56	29083192
185	Phosphorylation	AFLHPEEYDYMKDIV HHCCHHHHHHHHHHH	15.65	29083192
187	Phosphorylation	LHPEEYDYMKDIVVQ CCHHHHHHHHHHHHH	12.74	-
188	Sulfoxidation	HPEEYDYMKDIVVQE CHHHHHHHHHHHHHH	2.62	30846556
196	Phosphorylation	KDIVVQETMEDIDKN HHHHHHHHHHHHHHC	14.58	23663014
197	Sulfoxidation	DIVVQETMEDIDKNA HHHHHHHHHHHHHCC	4.24	28465586
213 (in isoform 10)	Phosphorylation	-	10.79	23663014
217	Sulfoxidation	LEEYIGDMYSHDGNT HHHHHHHHCCCCCCC	2.89	30846556
219 (in isoform 10)	Phosphorylation	-	14.41	23663014
224	Phosphorylation	MYSHDGNTDEPEWVK HCCCCCCCCCCHHHH	47.47	-
224	O-linked_Glycosylation	MYSHDGNTDEPEWVK HCCCCCCCCCCHHHH	47.47	OGP
248	Methylation	RDKNRDGKMDKEETK HHCCCCCCCCHHHHC	48.49	-
249	Sulfoxidation	DKNRDGKMDKEETKD HCCCCCCCCHHHHCC	12.45	30846556
254	Phosphorylation	GKMDKEETKDWILPS CCCCHHHHCCCCCCC	35.08	23917254
255	Ubiquitination	KMDKEETKDWILPSD CCCHHHHCCCCCCCC	55.11	2189047
255	Acetylation	KMDKEETKDWILPSD CCCHHHHCCCCCCCC	55.11	26051181
255 (in isoform 2)	Ubiquitination	-	55.11	21890473
261	Phosphorylation	TKDWILPSDYDHAEA HCCCCCCCCCCHHHH	45.41	20873877
261	O-linked_Glycosylation	TKDWILPSDYDHAEA HCCCCCCCCCCHHHH	45.41	62171197
263	Phosphorylation	DWILPSDYDHAEAEA CCCCCCCCCHHHHHH	17.61	23186163
263	Ubiquitination	DWILPSDYDHAEAEA CCCCCCCCCHHHHHH	17.61	21890473
275	Phosphorylation	AEARHLVYESDQNKD HHHHHHHHHCCCCCC	18.97	25884760
275	Nitration	AEARHLVYESDQNKD HHHHHHHHHCCCCCC	18.97	-
277	Phosphorylation	ARHLVYESDQNKDGK HHHHHHHCCCCCCCC	27.15	28152594
281	Ubiquitination	VYESDQNKDGKLTKE HHHCCCCCCCCCCHH	63.32	-
287	Sumoylation	NKDGKLTKEEIVDKY CCCCCCCHHHHHHHH	64.88	-
287	Sumoylation	NKDGKLTKEEIVDKY CCCCCCCHHHHHHHH	64.88	-
287	Ubiquitination	NKDGKLTKEEIVDKY CCCCCCCHHHHHHHH	64.88	-
293	Ubiquitination	TKEEIVDKYDLFVGS CHHHHHHHHCEEEEC	29.75	-
300	Phosphorylation	KYDLFVGSQATDFGE HHCEEEECCCCCHHH	16.02	23663014
300	O-linked_Glycosylation	KYDLFVGSQATDFGE HHCEEEECCCCCHHH	16.02	OGP
303	Phosphorylation	LFVGSQATDFGEALV EEEECCCCCHHHHHH	24.99	23663014
303	O-linked_Glycosylation	LFVGSQATDFGEALV EEEECCCCCHHHHHH	24.99	OGP

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
44	S	Phosphorylation	Kinase	PLK2	Q9NYY3	PSP
44	S	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
60	T	Phosphorylation	Kinase	PLK2	Q9NYY3	PSP
60	T	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
69	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
73	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
177	T	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
196	T	Phosphorylation	Kinase	PLK2	Q9NYY3	PSP
196	T	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
254	T	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAMP_HUMAN	APCS	physical	10631319
LYAG_HUMAN	GAA	physical	22939629
SYSM_HUMAN	SARS2	physical	22939629
TM256_HUMAN	TMEM256	physical	22939629
FAF2_HUMAN	FAF2	physical	22939629
PTBP3_HUMAN	PTBP3	physical	22939629
DREB_HUMAN	DBN1	physical	22939629
EMC1_HUMAN	EMC1	physical	22939629
ICT1_HUMAN	ICT1	physical	22939629
TM165_HUMAN	TMEM165	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
PERI_HUMAN	PRPH	physical	22939629
PPT2_HUMAN	PPT2	physical	22939629
EGFR_HUMAN	EGFR	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
SYIM_HUMAN	IARS2	physical	22939629
CAVN3_HUMAN	PRKCDBP	physical	22939629
CTNL1_HUMAN	CTNNAL1	physical	21988832
UMPS_HUMAN	UMPS	physical	21988832
ZPBP1_HUMAN	ZPBP	physical	21988832
ANM5_HUMAN	PRMT5	physical	23455924
SYAC_HUMAN	AARS	physical	22863883
AASD1_HUMAN	AARSD1	physical	22863883
ARC1B_HUMAN	ARPC1B	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
ARPC3_HUMAN	ARPC3	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
ARP5L_HUMAN	ARPC5L	physical	22863883
DPP8_HUMAN	DPP8	physical	22863883
EF2K_HUMAN	EEF2K	physical	22863883
HSF1_HUMAN	HSF1	physical	22863883
IPO11_HUMAN	IPO11	physical	22863883
KBP_HUMAN	KIAA1279	physical	22863883
METH_HUMAN	MTR	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
KAPCA_HUMAN	PRKACA	physical	22863883
KAP1_HUMAN	PRKAR1B	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
TM10A_HUMAN	TRMT10A	physical	22863883
RFA2_HUMAN	RPA2	physical	22863883
RPR1B_HUMAN	RPRD1B	physical	22863883
SAE1_HUMAN	SAE1	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
SHLB2_HUMAN	SH3GLB2	physical	22863883
THG1_HUMAN	THG1L	physical	22863883
PRPK_HUMAN	TP53RK	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UBQL1_HUMAN	UBQLN1	physical	25416956
OBSL1_HUMAN	OBSL1	physical	26186194
CALR_HUMAN	CALR	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
HS74L_HUMAN	HSPA4L	physical	26344197
NACA2_HUMAN	NACA2	physical	26344197
TKT_HUMAN	TKT	physical	26344197
HIC2_HUMAN	HIC2	physical	28514442

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 CALU_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131, AND MASSSPECTROMETRY.	19159218 [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-35, AND MASSSPECTROMETRY.	19413330 [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-44 AND THR-65, AND MASSSPECTROMETRY.	18691976 [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-44, AND MASSSPECTROMETRY.	17081983 [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 THR-65, AND MASSSPECTROMETRY.	16964243 [Abstract]