dbPTM

SRP72_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRP72_HUMAN
UniProt AC	O76094
Protein Name	Signal recognition particle subunit SRP72
Gene Name	SRP72
Organism	Homo sapiens (Human).
Sequence Length	671
Subcellular Localization	Cytoplasm . Endoplasmic reticulum .
Protein Description	Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function..
Protein Sequence	MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHELCYNTACALIGQGQLNQAMKILQKAEDLCRRSLSEDTDGTEEDPQAELAIIHGQMAYILQLQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFKLSKKQLQAIEFNKALLAMYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKAIELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYSHEEDIDSAIEVFTQAIQWYQNHQPKSPAHLSLIREAANFKLKYGRKKEAISDLQQLWKQNPKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSAGATYIRKKGGKVTGDSQPKEQGQGDLKKKKKKKKGKLPKNYDPKVTPDPERWLPMRERSYYRGRKKGKKKDQIGKGTQGATAGASSELDASKTVSSPPTSPRPGSAATVSASTSNIIPPRHQKPAGAPATKKKQQQKKKKGGKGGW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGGSGGV ------CCCCCCCCC	19.51	22223895
3	Phosphorylation	-----MASGGSGGVS -----CCCCCCCCCC	42.25	24850871
6	Phosphorylation	--MASGGSGGVSVPA --CCCCCCCCCCHHH	35.58	25159151
32	Acetylation	GDFTRALKTVNKILQ CCHHHHHHHHHHHHC	49.82	25953088
32	Ubiquitination	GDFTRALKTVNKILQ CCHHHHHHHHHHHHC	49.82	-
36	Acetylation	RALKTVNKILQINKD HHHHHHHHHHCCCHH	40.22	25953088
36	Malonylation	RALKTVNKILQINKD HHHHHHHHHHCCCHH	40.22	26320211
42	2-Hydroxyisobutyrylation	NKILQINKDDVTALH HHHHCCCHHCCHHHH	57.86	-
42	Acetylation	NKILQINKDDVTALH HHHHCCCHHCCHHHH	57.86	23749302
42	Ubiquitination	NKILQINKDDVTALH HHHHCCCHHCCHHHH	57.86	-
51	Acetylation	DVTALHCKVVCLIQN CCHHHHCEEEEEEEC	27.27	23236377
62	Acetylation	LIQNGSFKEALNVIN EEECCCHHHHHHHHH	43.72	25953088
73	Ubiquitination	NVINTHTKVLANNSL HHHHHHHHHHCCCCC	27.87	21890473
73	Ubiquitination	NVINTHTKVLANNSL HHHHHHHHHHCCCCC	27.87	21890473
81	Phosphorylation	VLANNSLSFEKAYCE HHCCCCCCHHHHHHH	31.05	25159151
84	Acetylation	NNSLSFEKAYCEYRL CCCCCHHHHHHHHHH	42.52	25953088
84	Ubiquitination	NNSLSFEKAYCEYRL CCCCCHHHHHHHHHH	42.52	21890473
84	Ubiquitination	NNSLSFEKAYCEYRL CCCCCHHHHHHHHHH	42.52	21890473
90	Methylation	EKAYCEYRLNRIENA HHHHHHHHHHHHHHH	11.82	115917797
99	Acetylation	NRIENALKTIESANQ HHHHHHHHHHHHHHH	45.08	25953088
99	Ubiquitination	NRIENALKTIESANQ HHHHHHHHHHHHHHH	45.08	21906983
100	Phosphorylation	RIENALKTIESANQQ HHHHHHHHHHHHHHH	30.72	23403867
103	Phosphorylation	NALKTIESANQQTDK HHHHHHHHHHHHHHH	28.77	23403867
108	Phosphorylation	IESANQQTDKLKELY HHHHHHHHHHHHHHH	25.90	19664995
110	2-Hydroxyisobutyrylation	SANQQTDKLKELYGQ HHHHHHHHHHHHHHH	65.92	-
110	Acetylation	SANQQTDKLKELYGQ HHHHHHHHHHHHHHH	65.92	26051181
110	Ubiquitination	SANQQTDKLKELYGQ HHHHHHHHHHHHHHH	65.92	-
112	2-Hydroxyisobutyrylation	NQQTDKLKELYGQVL HHHHHHHHHHHHHHH	51.95	-
112	Ubiquitination	NQQTDKLKELYGQVL HHHHHHHHHHHHHHH	51.95	21890473
112	Ubiquitination	NQQTDKLKELYGQVL HHHHHHHHHHHHHHH	51.95	21890473
115	Phosphorylation	TDKLKELYGQVLYRL HHHHHHHHHHHHHHH	13.45	27642862
125	Phosphorylation	VLYRLERYDECLAVY HHHHHHCHHHHHHHH	13.50	23879269
201	Acetylation	QAMKILQKAEDLCRR HHHHHHHHHHHHHHH	50.74	23236377
201	Malonylation	QAMKILQKAEDLCRR HHHHHHHHHHHHHHH	50.74	26320211
201	Ubiquitination	QAMKILQKAEDLCRR HHHHHHHHHHHHHHH	50.74	-
242	Phosphorylation	ILQLQGRTEEALQLY HHHHCCCHHHHHHHH	45.03	21712546
249	Phosphorylation	TEEALQLYNQIIKLK HHHHHHHHHHHHCCC	7.64	28152594
258	Phosphorylation	QIIKLKPTDVGLLAV HHHCCCCCCHHHHHH	41.55	20068231
272	Phosphorylation	VIANNIITINKDQNV HHHCCCEEECCCCCC	18.07	20068231
283	2-Hydroxyisobutyrylation	DQNVFDSKKKVKLTN CCCCCCCCCCEEECC	59.46	-
283	Acetylation	DQNVFDSKKKVKLTN CCCCCCCCCCEEECC	59.46	27452117
283	Succinylation	DQNVFDSKKKVKLTN CCCCCCCCCCEEECC	59.46	23954790
287	2-Hydroxyisobutyrylation	FDSKKKVKLTNAEGV CCCCCCEEECCCCCC	59.48	-
287	Acetylation	FDSKKKVKLTNAEGV CCCCCCEEECCCCCC	59.48	25953088
287	Ubiquitination	FDSKKKVKLTNAEGV CCCCCCEEECCCCCC	59.48	-
297	Ubiquitination	NAEGVEFKLSKKQLQ CCCCCEEECCHHHHH	38.04	-
301	Ubiquitination	VEFKLSKKQLQAIEF CEEECCHHHHHHHHH	53.52	-
323	Glutathionylation	YTNQAEQCRKISASL HCCHHHHHHHHHHHH	3.44	22555962
325	Ubiquitination	NQAEQCRKISASLQS CHHHHHHHHHHHHHC	48.95	-
352	Ubiquitination	AAQLCREKQHTKAIE HHHHHHHHHHHHHHH	28.20	-
356	Ubiquitination	CREKQHTKAIELLQE HHHHHHHHHHHHHHH	45.29	-
376	Ubiquitination	PENAAEIKLTMAQLK CCCHHHHHHHHHHHH	29.43	21906983
383	Acetylation	KLTMAQLKISQGNIS HHHHHHHHHCCCCHH	28.38	25953088
383	Malonylation	KLTMAQLKISQGNIS HHHHHHHHHCCCCHH	28.38	26320211
383	Ubiquitination	KLTMAQLKISQGNIS HHHHHHHHHCCCCHH	28.38	21890473
383	Ubiquitination	KLTMAQLKISQGNIS HHHHHHHHHCCCCHH	28.38	21890473
391	Acetylation	ISQGNISKACLILRS HCCCCHHHHHHHHHC	39.04	25953088
391	Malonylation	ISQGNISKACLILRS HCCCCHHHHHHHHHC	39.04	26320211
391	Sumoylation	ISQGNISKACLILRS HCCCCHHHHHHHHHC	39.04	25114211
391	Ubiquitination	ISQGNISKACLILRS HCCCCHHHHHHHHHC	39.04	-
443	Phosphorylation	YQNHQPKSPAHLSLI HHHCCCCCHHHHHHH	33.72	20873877
448	Phosphorylation	PKSPAHLSLIREAAN CCCHHHHHHHHHHHH	16.34	23312004
457	Acetylation	IREAANFKLKYGRKK HHHHHHCCCCCCCHH	43.83	25953088
463	Ubiquitination	FKLKYGRKKEAISDL CCCCCCCHHHHHHHH	51.07	-
464	Ubiquitination	KLKYGRKKEAISDLQ CCCCCCHHHHHHHHH	51.52	-
475	Acetylation	SDLQQLWKQNPKDIH HHHHHHHHHCHHHHH	49.11	23954790
475	Malonylation	SDLQQLWKQNPKDIH HHHHHHHHHCHHHHH	49.11	26320211
475	Ubiquitination	SDLQQLWKQNPKDIH HHHHHHHHHCHHHHH	49.11	21890473
475	Ubiquitination	SDLQQLWKQNPKDIH HHHHHHHHHCHHHHH	49.11	21890473
479	Ubiquitination	QLWKQNPKDIHTLAQ HHHHHCHHHHHHHHH	76.49	-
483	Phosphorylation	QNPKDIHTLAQLISA HCHHHHHHHHHHHHH	24.91	20860994
498	2-Hydroxyisobutyrylation	YSLVDPEKAKALSKH HHCCCHHHHHHHHHH	61.65	-
498	Acetylation	YSLVDPEKAKALSKH HHCCCHHHHHHHHHH	61.65	23236377
498	Ubiquitination	YSLVDPEKAKALSKH HHCCCHHHHHHHHHH	61.65	-
500	Ubiquitination	LVDPEKAKALSKHLP CCCHHHHHHHHHHCC	62.01	-
504	Acetylation	EKAKALSKHLPSSDS HHHHHHHHHCCCCCC	50.43	25953088
504	Malonylation	EKAKALSKHLPSSDS HHHHHHHHHCCCCCC	50.43	26320211
504	Ubiquitination	EKAKALSKHLPSSDS HHHHHHHHHCCCCCC	50.43	21890473
504	Ubiquitination	EKAKALSKHLPSSDS HHHHHHHHHCCCCCC	50.43	21890473
508	Phosphorylation	ALSKHLPSSDSMSLK HHHHHCCCCCCCCEE	53.81	27251275
509	Phosphorylation	LSKHLPSSDSMSLKV HHHHCCCCCCCCEEE	31.59	21601212
511	Phosphorylation	KHLPSSDSMSLKVDV HHCCCCCCCCEEECH	16.54	27251275
512	Sulfoxidation	HLPSSDSMSLKVDVE HCCCCCCCCEEECHH	6.98	30846556
515	Ubiquitination	SSDSMSLKVDVEALE CCCCCCEEECHHHHH	29.14	-
524	Phosphorylation	DVEALENSAGATYIR CHHHHHHCCCCCEEE	20.78	30108239
528	Phosphorylation	LENSAGATYIRKKGG HHHCCCCCEEEECCC	20.68	25849741
529	Phosphorylation	ENSAGATYIRKKGGK HHCCCCCEEEECCCE	9.74	21406692
538	Phosphorylation	RKKGGKVTGDSQPKE EECCCEECCCCCCCC	38.46	28450419
541	Phosphorylation	GGKVTGDSQPKEQGQ CCEECCCCCCCCCCC	50.13	29632367
544	Ubiquitination	VTGDSQPKEQGQGDL ECCCCCCCCCCCCCH	55.84	-
566	Phosphorylation	KGKLPKNYDPKVTPD CCCCCCCCCCCCCCC	39.48	30266825
569	Ubiquitination	LPKNYDPKVTPDPER CCCCCCCCCCCCHHH	56.71	-
571	Phosphorylation	KNYDPKVTPDPERWL CCCCCCCCCCHHHCC	28.27	23401153
594	Ubiquitination	RGRKKGKKKDQIGKG CCCCCCCCCCCCCCC	70.96	-
595	Ubiquitination	GRKKGKKKDQIGKGT CCCCCCCCCCCCCCC	59.35	-
600	Ubiquitination	KKKDQIGKGTQGATA CCCCCCCCCCCCCCC	61.49	2190698
602	Phosphorylation	KDQIGKGTQGATAGA CCCCCCCCCCCCCCC	27.58	20068231
606	Phosphorylation	GKGTQGATAGASSEL CCCCCCCCCCCCCCC	32.23	25262027
610	Phosphorylation	QGATAGASSELDASK CCCCCCCCCCCCCCC	24.35	25159151
611	Phosphorylation	GATAGASSELDASKT CCCCCCCCCCCCCCC	41.46	25159151
616	Phosphorylation	ASSELDASKTVSSPP CCCCCCCCCCCCCCC	28.64	25159151
618	Phosphorylation	SELDASKTVSSPPTS CCCCCCCCCCCCCCC	24.11	23927012
620	Phosphorylation	LDASKTVSSPPTSPR CCCCCCCCCCCCCCC	42.21	25159151
621	Phosphorylation	DASKTVSSPPTSPRP CCCCCCCCCCCCCCC	30.48	25159151
624	Phosphorylation	KTVSSPPTSPRPGSA CCCCCCCCCCCCCCC	55.54	25159151
625	Phosphorylation	TVSSPPTSPRPGSAA CCCCCCCCCCCCCCC	25.37	23927012
630	Phosphorylation	PTSPRPGSAATVSAS CCCCCCCCCCEECCC	19.88	23927012
633	Phosphorylation	PRPGSAATVSASTSN CCCCCCCEECCCCCC	18.08	23927012
635	Phosphorylation	PGSAATVSASTSNII CCCCCEECCCCCCCC	16.49	23927012
637	Phosphorylation	SAATVSASTSNIIPP CCCEECCCCCCCCCC	25.51	30278072
638	Phosphorylation	AATVSASTSNIIPPR CCEECCCCCCCCCCC	26.05	30278072
639	Phosphorylation	ATVSASTSNIIPPRH CEECCCCCCCCCCCC	24.44	30278072
655	O-linked_Glycosylation	KPAGAPATKKKQQQK CCCCCCCCHHHHHHH	42.19	28510447
655	Phosphorylation	KPAGAPATKKKQQQK CCCCCCCCHHHHHHH	42.19	26074081
656	Acetylation	PAGAPATKKKQQQKK CCCCCCCHHHHHHHH	61.14	24469395

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 SRP72_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRP72_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 SRP72_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KI21A_HUMAN	KIF21A	physical	22863883
MLF2_HUMAN	MLF2	physical	22863883
DDX54_HUMAN	DDX54	physical	26344197
GNL3L_HUMAN	GNL3L	physical	26344197
RRP12_HUMAN	RRP12	physical	26344197
SRP68_HUMAN	SRP68	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614675	Bone marrow failure syndrome 1 (BMFS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SRP72_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 THR-618 AND SER-620, ANDMASS SPECTROMETRY.	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 TYR-566; THR-571; THR-618AND SER-620, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, AND MASSSPECTROMETRY.	19690332 [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 THR-571, AND MASSSPECTROMETRY.	18691976 [Abstract]