dbPTM

SRP54_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRP54_HUMAN
UniProt AC	P61011
Protein Name	Signal recognition particle 54 kDa protein
Gene Name	SRP54
Organism	Homo sapiens (Human).
Sequence Length	504
Subcellular Localization	Nucleus speckle . Cytoplasm .
Protein Description	Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein)..
Protein Sequence	MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Dimethylation	MVLADLGRKITSALR CCCHHHHHHHHHHHH	34.20	-
8	Methylation	MVLADLGRKITSALR CCCHHHHHHHHHHHH	34.20	115372815
9	Ubiquitination	VLADLGRKITSALRS CCHHHHHHHHHHHHH	48.84	24816145
9	2-Hydroxyisobutyrylation	VLADLGRKITSALRS CCHHHHHHHHHHHHH	48.84	-
11	Phosphorylation	ADLGRKITSALRSLS HHHHHHHHHHHHHHH	15.81	20068231
12	Phosphorylation	DLGRKITSALRSLSN HHHHHHHHHHHHHHC	28.87	20068231
16	Phosphorylation	KITSALRSLSNATII HHHHHHHHHHCCCCC	36.68	30108239
18	Phosphorylation	TSALRSLSNATIINE HHHHHHHHCCCCCCH	26.18	26657352
21	Phosphorylation	LRSLSNATIINEEVL HHHHHCCCCCCHHHH	27.00	26657352
22	Ubiquitination	RSLSNATIINEEVLN HHHHCCCCCCHHHHH	2.71	32015554
24	Ubiquitination	LSNATIINEEVLNAM HHCCCCCCHHHHHHH	35.21	29967540
32	Ubiquitination	EEVLNAMLKEVCTAL HHHHHHHHHHHHHHH	3.88	29967540
32	Acetylation	EEVLNAMLKEVCTAL HHHHHHHHHHHHHHH	3.88	19608861
33	Acetylation	EVLNAMLKEVCTALL HHHHHHHHHHHHHHH	34.71	7676433
36	Ubiquitination	NAMLKEVCTALLEAD HHHHHHHHHHHHHCH	1.61	29967540
43	Ubiquitination	CTALLEADVNIKLVK HHHHHHCHHHHHHHH	25.31	23000965
47	Ubiquitination	LEADVNIKLVKQLRE HHCHHHHHHHHHHHH	41.86	22817900
49	Ubiquitination	ADVNIKLVKQLRENV CHHHHHHHHHHHHHH	2.93	23000965
50	Acetylation	DVNIKLVKQLRENVK HHHHHHHHHHHHHHH	54.79	7676443
50	Ubiquitination	DVNIKLVKQLRENVK HHHHHHHHHHHHHHH	54.79	21906983
57	Ubiquitination	KQLRENVKSAIDLEE HHHHHHHHHHCCHHH	45.83	24816145
57	Malonylation	KQLRENVKSAIDLEE HHHHHHHHHHCCHHH	45.83	26320211
58	Phosphorylation	QLRENVKSAIDLEEM HHHHHHHHHCCHHHH	26.61	-
65	Sulfoxidation	SAIDLEEMASGLNKR HHCCHHHHHHCCCHH	2.34	21406390
67	Phosphorylation	IDLEEMASGLNKRKM CCHHHHHHCCCHHHH	42.37	22210691
71	Ubiquitination	EMASGLNKRKMIQHA HHHHCCCHHHHHHHH	59.44	32015554
71	2-Hydroxyisobutyrylation	EMASGLNKRKMIQHA HHHHCCCHHHHHHHH	59.44	-
73	Ubiquitination	ASGLNKRKMIQHAVF HHCCCHHHHHHHHHH	41.80	29967540
81	Acetylation	MIQHAVFKELVKLVD HHHHHHHHHHHHHHC	43.47	19608861
81	Ubiquitination	MIQHAVFKELVKLVD HHHHHHHHHHHHHHC	43.47	19608861
85	Ubiquitination	AVFKELVKLVDPGVK HHHHHHHHHHCCCCC	56.25	29967540
85	Acetylation	AVFKELVKLVDPGVK HHHHHHHHHHCCCCC	56.25	25953088
92	Ubiquitination	KLVDPGVKAWTPTKG HHHCCCCCCCCCCCC	44.09	23000965
98	Ubiquitination	VKAWTPTKGKQNVIM CCCCCCCCCCCCEEE	66.37	23000965
100	Ubiquitination	AWTPTKGKQNVIMFV CCCCCCCCCCEEEEE	40.01	29967540
116	Phosphorylation	LQGSGKTTTCSKLAY ECCCCCCCCHHHHHH	29.32	28348404
117	Phosphorylation	QGSGKTTTCSKLAYY CCCCCCCCHHHHHHH	21.73	28348404
119	Phosphorylation	SGKTTTCSKLAYYYQ CCCCCCHHHHHHHHH	28.72	28348404
120	Acetylation	GKTTTCSKLAYYYQR CCCCCHHHHHHHHHH	39.00	26051181
149	Ubiquitination	AGAFDQLKQNATKAR CCHHHHHHHHCHHCC	35.55	29967540
149	Acetylation	AGAFDQLKQNATKAR CCHHHHHHHHCHHCC	35.55	26051181
160	Phosphorylation	TKARIPFYGSYTEMD HHCCCCCCCCCCCCC	10.37	29496907
162	Phosphorylation	ARIPFYGSYTEMDPV CCCCCCCCCCCCCCE	19.94	29496907
178	Acetylation	IASEGVEKFKNENFE EEECCHHHHCCCCEE	60.27	26051181
191	Phosphorylation	FEIIIVDTSGRHKQE EEEEEEECCCCCCCC	23.37	24719451
192	Phosphorylation	EIIIVDTSGRHKQED EEEEEECCCCCCCCC	29.39	27251275
200	Phosphorylation	GRHKQEDSLFEEMLQ CCCCCCCCHHHHHHH	33.92	24043423
202	Ubiquitination	HKQEDSLFEEMLQVA CCCCCCHHHHHHHHH	9.64	22817900
207	Ubiquitination	SLFEEMLQVANAIQP CHHHHHHHHHHHHCC	30.85	22817900
217	Ubiquitination	NAIQPDNIVYVMDAS HHHCCCCEEEEEECC	2.85	21890473
219	Ubiquitination	IQPDNIVYVMDASIG HCCCCEEEEEECCHH	6.05	23000965
219	Phosphorylation	IQPDNIVYVMDASIG HCCCCEEEEEECCHH	6.05	24043423
224	Phosphorylation	IVYVMDASIGQACEA EEEEEECCHHHHHHH	24.00	24043423
239	2-Hydroxyisobutyrylation	QAKAFKDKVDVASVI HHHHHHCCCCEEEEE	40.71	-
257	Ubiquitination	LDGHAKGGGALSAVA ECCCCCCCCHHHHHH	19.93	32015554
262	Ubiquitination	KGGGALSAVAATKSP CCCCHHHHHHHCCCC	8.87	33845483
267	Ubiquitination	LSAVAATKSPIIFIG HHHHHHCCCCEEEEE	49.89	-
272	Ubiquitination	ATKSPIIFIGTGEHI HCCCCEEEEECCCCC	4.34	23000965
272	Ubiquitination	ATKSPIIFIGTGEHI HCCCCEEEEECCCCC	4.34	21890473
274	Ubiquitination	KSPIIFIGTGEHIDD CCCEEEEECCCCCCC	19.54	23000965
294	Ubiquitination	TQPFISKLLGMGDIE CHHHHHHHHCCCCHH	3.89	24816145
297	Sulfoxidation	FISKLLGMGDIEGLI HHHHHHCCCCHHHHH	4.38	21406390
306	Ubiquitination	DIEGLIDKVNELKLD CHHHHHHHHHHCCCC	39.71	32015554
311	Ubiquitination	IDKVNELKLDDNEAL HHHHHHCCCCCCHHH	43.63	21906983
311	2-Hydroxyisobutyrylation	IDKVNELKLDDNEAL HHHHHHCCCCCCHHH	43.63	-
321	Ubiquitination	DNEALIEKLKHGQFT CCHHHHHHHHCCCEE	56.70	23000965
321	2-Hydroxyisobutyrylation	DNEALIEKLKHGQFT CCHHHHHHHHCCCEE	56.70	-
322	Ubiquitination	NEALIEKLKHGQFTL CHHHHHHHHCCCEEH	3.00	21890473
323	Ubiquitination	EALIEKLKHGQFTLR HHHHHHHHCCCEEHH	57.67	23000965
328	Phosphorylation	KLKHGQFTLRDMYEQ HHHCCCEEHHHHHHH	17.00	24719451
338	Ubiquitination	DMYEQFQNIMKMGPF HHHHHHHHHHHHCCH	37.30	23000965
344	Ubiquitination	QNIMKMGPFSQILGM HHHHHHCCHHHHHCC	23.40	23000965
349	Ubiquitination	MGPFSQILGMIPGFG HCCHHHHHCCCCCCC	2.71	24816145
353	Ubiquitination	SQILGMIPGFGTDFM HHHHCCCCCCCHHHH	24.14	23000965
360	Ubiquitination	PGFGTDFMSKGNEQE CCCCHHHHCCCCHHH	4.50	21890473
377	Ubiquitination	ARLKKLMTIMDSMND HHHHHHHHHHHHCCC	24.48	21890473
377	Ubiquitination	ARLKKLMTIMDSMND HHHHHHHHHHHHCCC	24.48	21890473
391	Ubiquitination	DQELDSTDGAKVFSK CCCCCCCCCCEECCC	60.03	22817900
392	Ubiquitination	QELDSTDGAKVFSKQ CCCCCCCCCEECCCC	27.64	23000965
393	Ubiquitination	ELDSTDGAKVFSKQP CCCCCCCCEECCCCC	13.98	23000965
398	Ubiquitination	DGAKVFSKQPGRIQR CCCEECCCCCCCEEE	49.39	24816145
398	Acetylation	DGAKVFSKQPGRIQR CCCEECCCCCCCEEE	49.39	27452117
399	Ubiquitination	GAKVFSKQPGRIQRV CCEECCCCCCCEEEH	44.47	23000965
400	Ubiquitination	AKVFSKQPGRIQRVA CEECCCCCCCEEEHH	37.45	23000965
407	Ubiquitination	PGRIQRVARGSGVST CCCEEEHHCCCCCCH	16.59	21890473
408	Ubiquitination	GRIQRVARGSGVSTR CCEEEHHCCCCCCHH	36.63	23000965
408	Ubiquitination	GRIQRVARGSGVSTR CCEEEHHCCCCCCHH	36.63	21890473
415	Ubiquitination	RGSGVSTRDVQELLT CCCCCCHHHHHHHHH	34.30	23000965
415	Ubiquitination	RGSGVSTRDVQELLT CCCCCCHHHHHHHHH	34.30	21890473
422	Phosphorylation	RDVQELLTQYTKFAQ HHHHHHHHHHHHHHH	31.96	28152594
424	Phosphorylation	VQELLTQYTKFAQMV HHHHHHHHHHHHHHH	13.48	28152594
425	Phosphorylation	QELLTQYTKFAQMVK HHHHHHHHHHHHHHH	15.18	28152594
426	Ubiquitination	ELLTQYTKFAQMVKK HHHHHHHHHHHHHHH	33.49	21906983
432	2-Hydroxyisobutyrylation	TKFAQMVKKMGGIKG HHHHHHHHHCCCCCC	31.53	-
432	Malonylation	TKFAQMVKKMGGIKG HHHHHHHHHCCCCCC	31.53	26320211
432	Acetylation	TKFAQMVKKMGGIKG HHHHHHHHHCCCCCC	31.53	25953088
438	Ubiquitination	VKKMGGIKGLFKGGD HHHCCCCCCHHCCCC	53.49	-
439	Ubiquitination	KKMGGIKGLFKGGDM HHCCCCCCHHCCCCC	34.13	23000965
442	Ubiquitination	GGIKGLFKGGDMSKN CCCCCHHCCCCCCCC	68.01	23000965
447	Ubiquitination	LFKGGDMSKNVSQSQ HHCCCCCCCCCCHHH	26.31	23000965
448	Ubiquitination	FKGGDMSKNVSQSQM HCCCCCCCCCCHHHH	55.52	23000965
451	Phosphorylation	GDMSKNVSQSQMAKL CCCCCCCCHHHHHHH	33.24	22798277
453	Phosphorylation	MSKNVSQSQMAKLNQ CCCCCCHHHHHHHHH	17.89	23312004
457	Ubiquitination	VSQSQMAKLNQQMAK CCHHHHHHHHHHHHH	42.50	23000965
464	Ubiquitination	KLNQQMAKMMDPRVL HHHHHHHHHCCHHHH	29.43	23000965
474	Sulfoxidation	DPRVLHHMGGMAGLQ CHHHHHHHHHHHHHH	3.27	30846556
477	Sulfoxidation	VLHHMGGMAGLQSMM HHHHHHHHHHHHHHH	1.90	30846556
482	Phosphorylation	GGMAGLQSMMRQFQQ HHHHHHHHHHHHHHH	21.42	28857561
483	Sulfoxidation	GMAGLQSMMRQFQQG HHHHHHHHHHHHHHH	1.33	30846556
484	Sulfoxidation	MAGLQSMMRQFQQGA HHHHHHHHHHHHHHC	3.54	30846556
496	Methylation	QGAAGNMKGMMGFNN HHCCCCCCCCCCCCC	47.88	54421941
496	Ubiquitination	QGAAGNMKGMMGFNN HHCCCCCCCCCCCCC	47.88	23000965

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 SRP54_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRP54_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 SRP54_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRP54_HUMAN	SRP54	physical	10497032
XRCC4_HUMAN	XRCC4	physical	22939629
TFAP4_HUMAN	TFAP4	physical	22939629
SRP68_HUMAN	SRP68	physical	23221635
SRP09_HUMAN	SRP9	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
SMC2_HUMAN	SMC2	physical	26344197
SMC4_HUMAN	SMC4	physical	26344197
SRP19_HUMAN	SRP19	physical	26344197
DERL1_HUMAN	DERL1	physical	26565908
DERL2_HUMAN	DERL2	physical	26565908

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 SRP54_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-81, AND MASS SPECTROMETRY.	19608861 [Abstract]