dbPTM

GO45_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GO45_HUMAN
UniProt AC	Q9H2G9
Protein Name	Golgin-45
Gene Name	BLZF1
Organism	Homo sapiens (Human).
Sequence Length	400
Subcellular Localization	Golgi apparatus lumen . Isoform 1: Nucleus. Isoform 2: Cytoplasm.
Protein Description	Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface..
Protein Sequence	MTTKNLETKVTVTSSPIRGAGDGMETEEPPKSVEVTSGVQSRKHHSLQSPWKKAVPSESPGVLQLGKMLTEKAMEVKAVRILVPKAAITHDIPNKNTKVKSLGHHKGEFLGQSEGVIEPNKELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQEMIATQKLLEELLVSLQWGREQTYSPSVQPHSTAELALTNHKLAKAVNSHLLGNVGINNQKKIPSTVEFCSTPAEKMAETVLRILDPVTCKESSPDNPFFESSPTTLLATKKNIGRFHPYTRYENITFNCCNHCRGELIAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTTKNLETK ------CCCCCCEEE	46.61	29449344
3	Phosphorylation	-----MTTKNLETKV -----CCCCCCEEEE	19.35	29449344
4	Ubiquitination	----MTTKNLETKVT ----CCCCCCEEEEE	50.82	33845483
8	Phosphorylation	MTTKNLETKVTVTSS CCCCCCEEEEEEECC	33.70	29449344
11	Phosphorylation	KNLETKVTVTSSPIR CCCEEEEEEECCCCC	21.44	28450419
13	Phosphorylation	LETKVTVTSSPIRGA CEEEEEEECCCCCCC	17.70	28102081
14	Phosphorylation	ETKVTVTSSPIRGAG EEEEEEECCCCCCCC	29.76	30266825
15	Phosphorylation	TKVTVTSSPIRGAGD EEEEEECCCCCCCCC	18.25	30266825
26	Phosphorylation	GAGDGMETEEPPKSV CCCCCCCCCCCCCCE	36.43	20068231
31	Ubiquitination	METEEPPKSVEVTSG CCCCCCCCCEEECCC	77.25	21906983
31 (in isoform 1)	Ubiquitination	-	77.25	21906983
31 (in isoform 2)	Ubiquitination	-	77.25	21906983
32	Phosphorylation	ETEEPPKSVEVTSGV CCCCCCCCEEECCCC	29.32	25159151
37	Phosphorylation	PKSVEVTSGVQSRKH CCCEEECCCCCCCCC	41.99	-
43	Ubiquitination	TSGVQSRKHHSLQSP CCCCCCCCCCCCCCC	51.41	29967540
49	Phosphorylation	RKHHSLQSPWKKAVP CCCCCCCCCHHHCCC	37.71	20068231
52	Ubiquitination	HSLQSPWKKAVPSES CCCCCCHHHCCCCCC	33.95	29967540
59	Phosphorylation	KKAVPSESPGVLQLG HHCCCCCCCCHHHHH	31.15	25159151
67	Ubiquitination	PGVLQLGKMLTEKAM CCHHHHHHHHHHHHH	39.05	21906983
67 (in isoform 2)	Ubiquitination	-	39.05	21906983
67 (in isoform 1)	Ubiquitination	-	39.05	21906983
70	Phosphorylation	LQLGKMLTEKAMEVK HHHHHHHHHHHHHHC	31.76	-
72 (in isoform 1)	Ubiquitination	-	48.04	21906983
72 (in isoform 2)	Ubiquitination	-	48.04	21906983
72	Ubiquitination	LGKMLTEKAMEVKAV HHHHHHHHHHHHCEE	48.04	21906983
77	Sumoylation	TEKAMEVKAVRILVP HHHHHHHCEEEEEEE	28.05	-
77	Sumoylation	TEKAMEVKAVRILVP HHHHHHHCEEEEEEE	28.05	-
77	Ubiquitination	TEKAMEVKAVRILVP HHHHHHHCEEEEEEE	28.05	22817900
85	Ubiquitination	AVRILVPKAAITHDI EEEEEEEHHHHCCCC	42.86	33845483
95	Ubiquitination	ITHDIPNKNTKVKSL HCCCCCCCCCCCEEC	61.72	29967540
106 (in isoform 1)	Ubiquitination	-	55.23	21906983
106 (in isoform 2)	Ubiquitination	-	55.23	21906983
106	Ubiquitination	VKSLGHHKGEFLGQS CEECCCCCCCHHCCC	55.23	21906983
121	Ubiquitination	EGVIEPNKELSEVKN CCCCCCCHHHHHHHH	71.41	29967540
127	Ubiquitination	NKELSEVKNVLEKLK CHHHHHHHHHHHHHH	36.97	29967540
127	Sumoylation	NKELSEVKNVLEKLK CHHHHHHHHHHHHHH	36.97	-
127	Sumoylation	NKELSEVKNVLEKLK CHHHHHHHHHHHHHH	36.97	-
144	Ubiquitination	ERRLLQDKEGLSNQL HHHHHHCHHHHCHHH	40.49	23503661
144 (in isoform 2)	Ubiquitination	-	40.49	-
156	Ubiquitination	NQLRVQTEVNRELKK HHHHHHHHHHHHHHH	22.24	21963094
176	Ubiquitination	VGDDLQYHFERLARE HCHHHHHHHHHHHHH	12.72	22817900
177	Ubiquitination	GDDLQYHFERLAREK CHHHHHHHHHHHHHH	5.07	22817900
184	Ubiquitination	FERLAREKNQLILEN HHHHHHHHCHHHHCC	44.43	29967540
184	2-Hydroxyisobutyrylation	FERLAREKNQLILEN HHHHHHHHCHHHHCC	44.43	-
198	Phosphorylation	NEALGRNTAQLSEQL CCCCCCCHHHHHHHH	17.89	22210691
222	Phosphorylation	WRSKFLASRVMADEL HHHHHHHHHHHHHHH	27.79	29083192
230	Phosphorylation	RVMADELTNSRAALQ HHHHHHHHHHHHHHH	29.15	29083192
232	Phosphorylation	MADELTNSRAALQRQ HHHHHHHHHHHHHHH	20.33	29083192
282	Phosphorylation	LQWGREQTYSPSVQP HHHCCCCCCCCCCCC	22.63	29214152
283	Phosphorylation	QWGREQTYSPSVQPH HHCCCCCCCCCCCCC	20.48	20068231
284	Phosphorylation	WGREQTYSPSVQPHS HCCCCCCCCCCCCCC	17.68	29496963
286	Phosphorylation	REQTYSPSVQPHSTA CCCCCCCCCCCCCHH	27.69	20068231
304	Ubiquitination	LTNHKLAKAVNSHLL HCHHHHHHHHHHHHH	64.40	29967540
320	Ubiquitination	NVGINNQKKIPSTVE CCCCCCCCCCCCCCE	55.59	29967540
321	Ubiquitination	VGINNQKKIPSTVEF CCCCCCCCCCCCCEE	50.51	29967540
324	Phosphorylation	NNQKKIPSTVEFCST CCCCCCCCCCEECCC	48.86	28857561
325	Phosphorylation	NQKKIPSTVEFCSTP CCCCCCCCCEECCCH	20.78	28857561
330	Phosphorylation	PSTVEFCSTPAEKMA CCCCEECCCHHHHHH	42.62	28555341
331	Phosphorylation	STVEFCSTPAEKMAE CCCEECCCHHHHHHH	27.91	21815630
339	Phosphorylation	PAEKMAETVLRILDP HHHHHHHHHHHHHCC	18.46	22210691
348	Phosphorylation	LRILDPVTCKESSPD HHHHCCCCCCCCCCC	24.21	18669648
350	Ubiquitination	ILDPVTCKESSPDNP HHCCCCCCCCCCCCC	51.79	21963094
352	Phosphorylation	DPVTCKESSPDNPFF CCCCCCCCCCCCCCC	32.44	22199227
353	Phosphorylation	PVTCKESSPDNPFFE CCCCCCCCCCCCCCC	37.05	26055452
361	Phosphorylation	PDNPFFESSPTTLLA CCCCCCCCCCCEEEE	36.14	25850435
362	Phosphorylation	DNPFFESSPTTLLAT CCCCCCCCCCEEEEE	21.04	26055452
364	Phosphorylation	PFFESSPTTLLATKK CCCCCCCCEEEEECC	31.83	22199227
365	Phosphorylation	FFESSPTTLLATKKN CCCCCCCEEEEECCC	24.14	22199227
369	Phosphorylation	SPTTLLATKKNIGRF CCCEEEEECCCCCCC	42.39	18669648
370 (in isoform 1)	Ubiquitination	-	37.91	21906983
370	Ubiquitination	PTTLLATKKNIGRFH CCEEEEECCCCCCCC	37.91	22817900
371	Ubiquitination	TTLLATKKNIGRFHP CEEEEECCCCCCCCC	49.82	22817900

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF146	Q9NTX7	PMID:21478859

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GO45_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 GO45_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GORS2_HUMAN	GORASP2	physical	11739402
ZZZ3_HUMAN	ZZZ3	physical	20211142
ZN410_HUMAN	ZNF410	physical	20211142
RN146_HUMAN	RNF146	physical	21478859
TNKS1_HUMAN	TNKS	physical	21478859
SRA1_HUMAN	SRA1	physical	20398657
GORS2_HUMAN	GORASP2	physical	21988832
KDM1A_HUMAN	KDM1A	physical	23455924
ANM6_HUMAN	PRMT6	physical	23455924
SUV92_HUMAN	SUV39H2	physical	23455924
ZBT24_HUMAN	ZBTB24	physical	25416956
AKAP9_HUMAN	AKAP9	physical	25416956
VPS28_HUMAN	VPS28	physical	25416956
TBCD7_HUMAN	TBC1D7	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
CINP_HUMAN	CINP	physical	25416956
OAZ3_HUMAN	OAZ3	physical	25416956
TPC2L_HUMAN	TRAPPC2L	physical	25416956
RB39A_HUMAN	RAB39A	physical	25416956
MIC19_HUMAN	CHCHD3	physical	25416956
RHOJ_HUMAN	RHOJ	physical	25416956
ZN410_HUMAN	ZNF410	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
SCNM1_HUMAN	SCNM1	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
TXND5_HUMAN	TXNDC5	physical	25416956
T22D4_HUMAN	TSC22D4	physical	25416956
ZMAT1_HUMAN	ZMAT1	physical	25416956
ZGPAT_HUMAN	ZGPAT	physical	25416956
BEX2_HUMAN	BEX2	physical	25416956
RAB2B_HUMAN	RAB2B	physical	25416956
FBF1_HUMAN	FBF1	physical	25416956
FRMD6_HUMAN	FRMD6	physical	25416956
IQUB_HUMAN	IQUB	physical	25416956
KLH38_HUMAN	KLHL38	physical	25416956
TNKS1_HUMAN	TNKS	physical	26186194
GORS2_HUMAN	GORASP2	physical	28514442
TNKS1_HUMAN	TNKS	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 GO45_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-15, 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-353 AND THR-369, ANDMASS SPECTROMETRY.	18669648 [Abstract]