PRSR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PRSR1_HUMAN
• UniProt AC: Q86XN7
• Protein Name: Proline and serine-rich protein 1
• Gene Name: PROSER1
• Organism: Homo sapiens (Human).
• Sequence Length: 944
• Protein Sequence: MDKKSFEMVLDEIRKAVLTEYKLKAIEYVHGYFSSEQVVDLLRYFSWAEPQLKAMKALQHKMVAVQPTEVVNILNCFTFSKDKLVALELLASNIIDAQNSRPIEDLFRVNMSEKKRCKRILEQAFKGGCKAPHAMISSCGTIPGNPYPKGRPSRINGIFPGTPLKKDGEECTNEGKGIAARILGPSKPPPSTYNPHKPVPYPIPPCRPHATIAPSAYNNAGLVPLANVIAPPPPPYTPNPVGTENEDLSNPSKPIQNQTFSTPASQLFSPHGSNPSTPAATPVPTASPVKAINHPSASAAATVSGMNLLNTVLPVFPGQVSSAVHTPQPSIPNPTVIRTPSLPTAPVTSIHSTTTTPVPSIFSGLVSLPGPSATPTAATPTPGPTPRSTLGSSEAFASTSAPFTSLPFSTSSSAASTSNPNSASLSSVFAGLPLPLPPTSQGLSNPTPVIAGGSTPSVAGPLGVNSPLLSALKGFLTSNDTNLINSSALSSAVTSGLASLSSLTLQNSDSSASAPNKCYAPSAIPTPQRTSTPGLALFPGLPSPVANSTSTPLTLPVQSPLATAASASTSVPVSCGSSASLLRGPHPGTSDLHISSTPAATTLPVMIKTEPTSPTPSAFKGPSHSGNPSHGTLGLSGTLGRAYTSTSVPISLSACLNPALSGLSSLSTPLNGSNPLSSISLPPHGSSTPIAPVFTALPSFTSLTNNFPLTGNPSLNPSVSLPGSLIATSSTAATSTSLPHPSSTAAVLSGLSASAPVSAAPFPLNLSTAVPSLFSVTQGPLSSSNPSYPGFSVSNTPSVTPALPSFPGLQAPSTVAAVTPLPVAATAPSPAPVLPGFASAFSSNFNSALVAQAGLSSGLQAAGSSVFPGLLSLPGIPGFPQNPSQSSLQELQHNAAAQSALLQQVHSASALESYPAQPDGFPSYPSAPGTPFSLQPSLSQSGWQ

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDKKSFEM -------CCHHHHHH	17.98	22814378
126	Acetylation	RILEQAFKGGCKAPH HHHHHHHCCCCCCCC	58.36	25953088
126	Ubiquitination	RILEQAFKGGCKAPH HHHHHHHCCCCCCCC	58.36	29967540
154	Ubiquitination	YPKGRPSRINGIFPG CCCCCCCCCCCCCCC	29.13	-
162	Phosphorylation	INGIFPGTPLKKDGE CCCCCCCCCCCCCCH	26.20	21815630
165	Acetylation	IFPGTPLKKDGEECT CCCCCCCCCCCHHCC	50.45	25953088
176	Ubiquitination	EECTNEGKGIAARIL HHCCCCCCCCCHHHH	40.75	-
176	Acetylation	EECTNEGKGIAARIL HHCCCCCCCCCHHHH	40.75	26051181
269	Phosphorylation	TPASQLFSPHGSNPS CCHHHHCCCCCCCCC	25.28	26074081
273	Phosphorylation	QLFSPHGSNPSTPAA HHCCCCCCCCCCCCC	42.40	26074081
276	Phosphorylation	SPHGSNPSTPAATPV CCCCCCCCCCCCCCC	51.80	26074081
277	Phosphorylation	PHGSNPSTPAATPVP CCCCCCCCCCCCCCC	20.43	26074081
281	Phosphorylation	NPSTPAATPVPTASP CCCCCCCCCCCCCCC	27.25	26074081
285	Phosphorylation	PAATPVPTASPVKAI CCCCCCCCCCCCCCC	39.75	27050516
287	Phosphorylation	ATPVPTASPVKAINH CCCCCCCCCCCCCCC	32.48	25159151
296	Phosphorylation	VKAINHPSASAAATV CCCCCCCCCCHHHHH	27.57	26074081
298	Phosphorylation	AINHPSASAAATVSG CCCCCCCCHHHHHHH	23.83	26074081
302	Phosphorylation	PSASAAATVSGMNLL CCCCHHHHHHHHHHH	15.52	26074081
304	Phosphorylation	ASAAATVSGMNLLNT CCHHHHHHHHHHHHH	28.15	26074081
526	Phosphorylation	YAPSAIPTPQRTSTP ECCCCCCCCCCCCCC	26.41	29396449
602	O-linked_Glycosylation	SSTPAATTLPVMIKT CCCCCCCCCCEEEEC	25.08	30059200
608	Sumoylation	TTLPVMIKTEPTSPT CCCCEEEECCCCCCC	28.83	-
609	Phosphorylation	TLPVMIKTEPTSPTP CCCEEEECCCCCCCC	35.95	29255136
612	Phosphorylation	VMIKTEPTSPTPSAF EEEECCCCCCCCCCC	40.90	30266825
613	Phosphorylation	MIKTEPTSPTPSAFK EEECCCCCCCCCCCC	37.18	23401153
615	Phosphorylation	KTEPTSPTPSAFKGP ECCCCCCCCCCCCCC	29.64	29255136
617	Phosphorylation	EPTSPTPSAFKGPSH CCCCCCCCCCCCCCC	49.14	29255136
625	Phosphorylation	AFKGPSHSGNPSHGT CCCCCCCCCCCCCCC	44.60	28464451
629	Phosphorylation	PSHSGNPSHGTLGLS CCCCCCCCCCCCCCC	38.25	28464451
638	Phosphorylation	GTLGLSGTLGRAYTS CCCCCCCCCCCCCCC	23.74	28555341
926	Phosphorylation	DGFPSYPSAPGTPFS CCCCCCCCCCCCCCC	38.57	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PRSR1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PRSR1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PRSR1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PRSR1_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-613, AND MASSSPECTROMETRY.
PubMed: 19413330