dbPTM

SMD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMD3_HUMAN
UniProt AC	P62318
Protein Name	Small nuclear ribonucleoprotein Sm D3
Gene Name	SNRPD3
Organism	Homo sapiens (Human).
Sequence Length	126
Subcellular Localization	Cytoplasm, cytosol . Nucleus . SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.
Protein Description	Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing..
Protein Sequence	MSIGVPIKVLHEAEGHIVTCETNTGEVYRGKLIEAEDNMNCQMSNITVTYRDGRVAQLEQVYIRGSKIRFLILPDMLKNAPMLKSMKNKNQGSGAGRGKAAILKAQVAARGRGRGMGRGNIFQKRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSIGVPIKV ------CCCCCCEEE	28.22	23401153
2	Acetylation	------MSIGVPIKV ------CCCCCCEEE	28.22	19413330
8	Sumoylation	MSIGVPIKVLHEAEG CCCCCCEEEEEECCC	32.45	-
8	2-Hydroxyisobutyrylation	MSIGVPIKVLHEAEG CCCCCCEEEEEECCC	32.45	-
8	Ubiquitination	MSIGVPIKVLHEAEG CCCCCCEEEEEECCC	32.45	-
8	Acetylation	MSIGVPIKVLHEAEG CCCCCCEEEEEECCC	32.45	-
8	Ubiquitination	MSIGVPIKVLHEAEG CCCCCCEEEEEECCC	32.45	-
8	Acetylation	MSIGVPIKVLHEAEG CCCCCCEEEEEECCC	32.45	23954790
20	S-nitrosylation	AEGHIVTCETNTGEV CCCEEEEEECCCCCE	4.15	25040305
20	Glutathionylation	AEGHIVTCETNTGEV CCCEEEEEECCCCCE	4.15	22555962
28	Phosphorylation	ETNTGEVYRGKLIEA ECCCCCEEECEEEEE	14.89	29496907
31	Acetylation	TGEVYRGKLIEAEDN CCCEEECEEEEEECC	36.97	26051181
44	Phosphorylation	DNMNCQMSNITVTYR CCCCCEECEEEEEEC	10.13	28176443
62	Phosphorylation	VAQLEQVYIRGSKIR EEEEEEEEECCCCEE	5.65	28152594
64	Methylation	QLEQVYIRGSKIRFL EEEEEEECCCCEEEE	26.16	115917397
66	Phosphorylation	EQVYIRGSKIRFLIL EEEEECCCCEEEEEC	18.30	30108239
76	Sulfoxidation	RFLILPDMLKNAPML EEEECHHHHHCCHHH	5.61	21406390
78	2-Hydroxyisobutyrylation	LILPDMLKNAPMLKS EECHHHHHCCHHHHH	44.41	-
78	Ubiquitination	LILPDMLKNAPMLKS EECHHHHHCCHHHHH	44.41	21906983
78	Acetylation	LILPDMLKNAPMLKS EECHHHHHCCHHHHH	44.41	-
78	Ubiquitination	LILPDMLKNAPMLKS EECHHHHHCCHHHHH	44.41	21963094
78	Acetylation	LILPDMLKNAPMLKS EECHHHHHCCHHHHH	44.41	23954790
84	Malonylation	LKNAPMLKSMKNKNQ HHCCHHHHHHCCCCC	42.10	26320211
84	Ubiquitination	LKNAPMLKSMKNKNQ HHCCHHHHHHCCCCC	42.10	-
84	Acetylation	LKNAPMLKSMKNKNQ HHCCHHHHHHCCCCC	42.10	25953088
84	Ubiquitination	LKNAPMLKSMKNKNQ HHCCHHHHHHCCCCC	42.10	32015554
87	Ubiquitination	APMLKSMKNKNQGSG CHHHHHHCCCCCCCC	72.38	-
93	Phosphorylation	MKNKNQGSGAGRGKA HCCCCCCCCCCCHHH	18.73	22817900
97	Methylation	NQGSGAGRGKAAILK CCCCCCCCHHHHHHH	42.79	80700925
97	Dimethylation	NQGSGAGRGKAAILK CCCCCCCCHHHHHHH	42.79	-
99	Methylation	GSGAGRGKAAILKAQ CCCCCCHHHHHHHHH	33.03	-
99	Methylation	GSGAGRGKAAILKAQ CCCCCCHHHHHHHHH	33.03	23748837
104	Ubiquitination	RGKAAILKAQVAARG CHHHHHHHHHHHHCC	30.57	32015554
110	Methylation	LKAQVAARGRGRGMG HHHHHHHCCCCCCCC	26.13	134919
110	Dimethylation	LKAQVAARGRGRGMG HHHHHHHCCCCCCCC	26.13	-
112	Methylation	AQVAARGRGRGMGRG HHHHHCCCCCCCCCC	26.53	134923
112	Dimethylation	AQVAARGRGRGMGRG HHHHHCCCCCCCCCC	26.53	-
114	Methylation	VAARGRGRGMGRGNI HHHCCCCCCCCCCCC	30.48	80700931
114	Dimethylation	VAARGRGRGMGRGNI HHHCCCCCCCCCCCC	30.48	-
118	Methylation	GRGRGMGRGNIFQKR CCCCCCCCCCCCCCC	26.54	80700937
118	Dimethylation	GRGRGMGRGNIFQKR CCCCCCCCCCCCCCC	26.54	-
124	2-Hydroxyisobutyrylation	GRGNIFQKRR----- CCCCCCCCCC-----	39.12	-

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
Oops, there are no upstream regulatory protein records of SMD3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SMD3_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 SMD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANM5_HUMAN	PRMT5	physical	11713266
ICLN_HUMAN	CLNS1A	physical	11713266
RSMN_HUMAN	SNRPN	physical	9417867
RUXE_HUMAN	SNRPE	physical	9417867
RUXG_HUMAN	SNRPG	physical	9417867
RSMB_HUMAN	SNRPB	physical	10025403
U520_HUMAN	SNRNP200	physical	22939629
U5S1_HUMAN	EFTUD2	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
SSRD_HUMAN	SSR4	physical	22939629
RSMB_HUMAN	SNRPB	physical	22365833
LSM3_HUMAN	LSM3	physical	22365833
LSM7_HUMAN	LSM7	physical	22365833
ICLN_HUMAN	CLNS1A	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
TRDMT_HUMAN	TRDMT1	physical	21988832
PHAR4_HUMAN	PHACTR4	physical	22863883
TF65_HUMAN	RELA	physical	22863883
AIMP1_HUMAN	AIMP1	physical	26344197
PRP16_HUMAN	DHX38	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
LSM2_HUMAN	LSM2	physical	26344197
LSM3_HUMAN	LSM3	physical	26344197
LSM6_HUMAN	LSM6	physical	26344197
LSM7_HUMAN	LSM7	physical	26344197
LC7L2_HUMAN	LUC7L2	physical	26344197
PRPF3_HUMAN	PRPF3	physical	26344197
RCC2_HUMAN	RCC2	physical	26344197
SF3A3_HUMAN	SF3A3	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
SMRCD_HUMAN	SMARCAD1	physical	26344197
U520_HUMAN	SNRNP200	physical	26344197
RU17_HUMAN	SNRNP70	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
RUXE_HUMAN	SNRPE	physical	26344197
RUXF_HUMAN	SNRPF	physical	26344197
RUXG_HUMAN	SNRPG	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 SMD3_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-97, AND MASS SPECTROMETRY.	15782174 [Abstract]