dbPTM

SRP09_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRP09_HUMAN
UniProt AC	P49458
Protein Name	Signal recognition particle 9 kDa protein
Gene Name	SRP9
Organism	Homo sapiens (Human).
Sequence Length	86
Subcellular Localization	Cytoplasm.
Protein Description	Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding..
Protein Sequence	MPQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGNLCVKVTDDLVCLVYKTDQAQDVKKIEKFHSQLMRLMVAKEARNVTMETE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPQYQTWEEFS ----CCCCCCHHHHH	11.31	25884760
6	Phosphorylation	--MPQYQTWEEFSRA --CCCCCCHHHHHHH	29.88	21406692
11	Phosphorylation	YQTWEEFSRAAEKLY CCCHHHHHHHHHHHH	25.04	21406692
16	Ubiquitination	EFSRAAEKLYLADPM HHHHHHHHHHCCCCC	37.39	21890473
16	Ubiquitination	EFSRAAEKLYLADPM HHHHHHHHHHCCCCC	37.39	21890473
16	Ubiquitination	EFSRAAEKLYLADPM HHHHHHHHHHCCCCC	37.39	21890473
16	Acetylation	EFSRAAEKLYLADPM HHHHHHHHHHCCCCC	37.39	23236377
16	Ubiquitination	EFSRAAEKLYLADPM HHHHHHHHHHCCCCC	37.39	21890473
16	2-Hydroxyisobutyrylation	EFSRAAEKLYLADPM HHHHHHHHHHCCCCC	37.39	-
18	Phosphorylation	SRAAEKLYLADPMKA HHHHHHHHCCCCCEE	15.77	29496907
23	Sulfoxidation	KLYLADPMKARVVLK HHHCCCCCEEEEEEE	5.66	30846556
24	2-Hydroxyisobutyrylation	LYLADPMKARVVLKY HHCCCCCEEEEEEEE	38.13	-
24	Ubiquitination	LYLADPMKARVVLKY HHCCCCCEEEEEEEE	38.13	21890473
24	Ubiquitination	LYLADPMKARVVLKY HHCCCCCEEEEEEEE	38.13	21906983
24	Ubiquitination	LYLADPMKARVVLKY HHCCCCCEEEEEEEE	38.13	21890473
24	Ubiquitination	LYLADPMKARVVLKY HHCCCCCEEEEEEEE	38.13	21890473
24	Acetylation	LYLADPMKARVVLKY HHCCCCCEEEEEEEE	38.13	25953088
30	Acetylation	MKARVVLKYRHSDGN CEEEEEEEEECCCCC	28.73	25825284
30	Ubiquitination	MKARVVLKYRHSDGN CEEEEEEEEECCCCC	28.73	19608861
31	Phosphorylation	KARVVLKYRHSDGNL EEEEEEEEECCCCCE	14.92	27251275
32	Methylation	ARVVLKYRHSDGNLC EEEEEEEECCCCCEE	22.65	115917801
34	Phosphorylation	VVLKYRHSDGNLCVK EEEEEECCCCCEEEE	37.91	29214152
39	S-nitrosylation	RHSDGNLCVKVTDDL ECCCCCEEEEECCCE	3.02	19483679
39	S-nitrosocysteine	RHSDGNLCVKVTDDL ECCCCCEEEEECCCE	3.02	-
41	Ubiquitination	SDGNLCVKVTDDLVC CCCCEEEEECCCEEE	38.12	-
41	Acetylation	SDGNLCVKVTDDLVC CCCCEEEEECCCEEE	38.12	23749302
41 (in isoform 2)	Ubiquitination	-	38.12	-
43	Phosphorylation	GNLCVKVTDDLVCLV CCEEEEECCCEEEEE	20.34	21712546
48	Glutathionylation	KVTDDLVCLVYKTDQ EECCCEEEEEEECCC	2.50	22555962
48	S-nitrosylation	KVTDDLVCLVYKTDQ EECCCEEEEEEECCC	2.50	19483679
48	S-nitrosocysteine	KVTDDLVCLVYKTDQ EECCCEEEEEEECCC	2.50	-
51	Nitration	DDLVCLVYKTDQAQD CCEEEEEEECCCHHH	8.67	-
52	Acetylation	DLVCLVYKTDQAQDV CEEEEEEECCCHHHH	37.84	19608861
52	Ubiquitination	DLVCLVYKTDQAQDV CEEEEEEECCCHHHH	37.84	19608861
52	2-Hydroxyisobutyrylation	DLVCLVYKTDQAQDV CEEEEEEECCCHHHH	37.84	-
60	Acetylation	TDQAQDVKKIEKFHS CCCHHHHHHHHHHHH	57.22	23749302
60	Ubiquitination	TDQAQDVKKIEKFHS CCCHHHHHHHHHHHH	57.22	-
60	Sumoylation	TDQAQDVKKIEKFHS CCCHHHHHHHHHHHH	57.22	-
61	Acetylation	DQAQDVKKIEKFHSQ CCHHHHHHHHHHHHH	56.81	25953088
61	Ubiquitination	DQAQDVKKIEKFHSQ CCHHHHHHHHHHHHH	56.81	21890473
61	Ubiquitination	DQAQDVKKIEKFHSQ CCHHHHHHHHHHHHH	56.81	21890473
64	Ubiquitination	QDVKKIEKFHSQLMR HHHHHHHHHHHHHHH	52.42	21890473
64	Acetylation	QDVKKIEKFHSQLMR HHHHHHHHHHHHHHH	52.42	25825284
64	Ubiquitination	QDVKKIEKFHSQLMR HHHHHHHHHHHHHHH	52.42	21890473
64	2-Hydroxyisobutyrylation	QDVKKIEKFHSQLMR HHHHHHHHHHHHHHH	52.42	-
71	Methylation	KFHSQLMRLMVAKEA HHHHHHHHHHHHHHH	28.37	115917805
75 (in isoform 2)	Phosphorylation	-	7.04	22210691
76	Ubiquitination	LMRLMVAKEARNVTM HHHHHHHHHHHCCCC	40.26	21890473
76	Ubiquitination	LMRLMVAKEARNVTM HHHHHHHHHHHCCCC	40.26	21890473
76	Malonylation	LMRLMVAKEARNVTM HHHHHHHHHHHCCCC	40.26	26320211
76	Acetylation	LMRLMVAKEARNVTM HHHHHHHHHHHCCCC	40.26	26051181
76	2-Hydroxyisobutyrylation	LMRLMVAKEARNVTM HHHHHHHHHHHCCCC	40.26	-
80 (in isoform 2)	Phosphorylation	-	40.43	22210691
82	Phosphorylation	AKEARNVTMETE--- HHHHHCCCCCCC---	16.91	27251275
83	Sulfoxidation	KEARNVTMETE---- HHHHCCCCCCC----	5.37	30846556
85	Phosphorylation	ARNVTMETE------ HHCCCCCCC------	35.85	28985074

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	RCHY1	Q96PM5	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRP09_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 SRP09_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRP14_HUMAN	SRP14	physical	11089964
SRP14_HUMAN	SRP14	physical	2153922
SRP14_HUMAN	SRP14	physical	22939629
TEBP_HUMAN	PTGES3	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
SRP68_HUMAN	SRP68	physical	23221635
SRP54_HUMAN	SRP54	physical	23221635
SRP14_HUMAN	SRP14	physical	23221635
SMN_HUMAN	SMN1	physical	23221635
GEMI2_HUMAN	GEMIN2	physical	23221635
DDX20_HUMAN	DDX20	physical	23221635
GEMI4_HUMAN	GEMIN4	physical	23221635
GEMI5_HUMAN	GEMIN5	physical	23221635
IL7RA_HUMAN	IL7R	physical	23151878
PLIN3_HUMAN	PLIN3	physical	22863883
RPR1A_HUMAN	RPRD1A	physical	22863883
SRP14_HUMAN	SRP14	physical	22863883
SRP54_HUMAN	SRP54	physical	28514442
TRM61_HUMAN	TRMT61A	physical	28514442
SRP68_HUMAN	SRP68	physical	28514442
SRP19_HUMAN	SRP19	physical	28514442
SRP14_HUMAN	SRP14	physical	28514442
SRP72_HUMAN	SRP72	physical	28514442
MTD2L_HUMAN	MTHFD2L	physical	28514442
EDA_HUMAN	EDA	physical	28514442
MTDC_HUMAN	MTHFD2	physical	28514442
TRM6_HUMAN	TRMT6	physical	28514442
RAD18_HUMAN	RAD18	physical	28514442
UBP4_HUMAN	USP4	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 SRP09_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-30 AND LYS-52, AND MASSSPECTROMETRY.	19608861 [Abstract]