dbPTM

PWP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PWP1_HUMAN
UniProt AC	Q13610
Protein Name	Periodic tryptophan protein 1 homolog
Gene Name	PWP1
Organism	Homo sapiens (Human).
Sequence Length	501
Subcellular Localization	Nucleus.
Protein Description	May play an important role in cell growth and/or transcription..
Protein Sequence	MNRSRQVTCVAWVRCGVAKETPDKVELSKEEVKRLIAEAKEKLQEEGGGSDEEETGSPSEDGMQSARTQARPREPLEDGDPEDDRTLDDDELAEYDLDKYDEEGDPDAETLGESLLGLTVYGSNDQDPYVTLKDTEQYEREDFLIKPSDNLIVCGRAEQDQCNLEVHVYNQEEDSFYVHHDILLSAYPLSVEWLNFDPSPDDSTGNYIAVGNMTPVIEVWDLDIVDSLEPVFTLGSKLSKKKKKKGKKSSSAEGHTDAVLDLSWNKLIRNVLASASADNTVILWDMSLGKPAASLAVHTDKVQTLQFHPFEAQTLISGSYDKSVALYDCRSPDESHRMWRFSGQIERVTWNHFSPCHFLASTDDGFVYNLDARSDKPIFTLNAHNDEISGLDLSSQIKGCLVTASADKYVKIWDILGDRPSLVHSRDMKMGVLFCSSCCPDLPFIYAFGGQKEGLRVWDISTVSSVNEAFGRRERLVLGSARNSSISGPFGSRSSDTPMES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNRSRQVT -------CCCCCCEE	9.43	-
19	Acetylation	WVRCGVAKETPDKVE EEEECCCCCCCCCCC	60.77	26051181
21	Phosphorylation	RCGVAKETPDKVELS EECCCCCCCCCCCCC	35.76	25159151
24	Ubiquitination	VAKETPDKVELSKEE CCCCCCCCCCCCHHH	38.52	-
28	Phosphorylation	TPDKVELSKEEVKRL CCCCCCCCHHHHHHH	25.23	23186163
29	Ubiquitination	PDKVELSKEEVKRLI CCCCCCCHHHHHHHH	71.20	-
33	Ubiquitination	ELSKEEVKRLIAEAK CCCHHHHHHHHHHHH	44.78	-
40	Ubiquitination	KRLIAEAKEKLQEEG HHHHHHHHHHHHHCC	47.06	21906983
40	Ubiquitination	KRLIAEAKEKLQEEG HHHHHHHHHHHHHCC	47.06	21906983
42	Ubiquitination	LIAEAKEKLQEEGGG HHHHHHHHHHHCCCC	55.55	-
50	Phosphorylation	LQEEGGGSDEEETGS HHHCCCCCCCCCCCC	45.16	19664994
55	Phosphorylation	GGSDEEETGSPSEDG CCCCCCCCCCCCHHH	46.36	22167270
57	Phosphorylation	SDEEETGSPSEDGMQ CCCCCCCCCCHHHHH	32.45	22167270
59	Phosphorylation	EEETGSPSEDGMQSA CCCCCCCCHHHHHHH	50.44	22167270
65	Phosphorylation	PSEDGMQSARTQARP CCHHHHHHHHHCCCC	15.72	22167270
85	Methylation	DGDPEDDRTLDDDEL CCCCCCCCCCCHHHH	49.89	115489699
86	Phosphorylation	GDPEDDRTLDDDELA CCCCCCCCCCHHHHH	41.35	25159151
110	Phosphorylation	EGDPDAETLGESLLG CCCCCHHHHHHHHCC	41.61	29523821
114	Phosphorylation	DAETLGESLLGLTVY CHHHHHHHHCCCEEE	27.39	20860994
119	Phosphorylation	GESLLGLTVYGSNDQ HHHHCCCEEECCCCC	15.19	29523821
121	Phosphorylation	SLLGLTVYGSNDQDP HHCCCEEECCCCCCC	15.03	-
129	Phosphorylation	GSNDQDPYVTLKDTE CCCCCCCCEEEECCC	17.85	-
133	Ubiquitination	QDPYVTLKDTEQYER CCCCEEEECCCHHCC	53.92	-
135	Phosphorylation	PYVTLKDTEQYERED CCEEEECCCHHCCCC	24.33	28796482
138	Phosphorylation	TLKDTEQYEREDFLI EEECCCHHCCCCCEE	15.66	28796482
249	Phosphorylation	KKKKGKKSSSAEGHT HHCCCCCCCCCCCCH	32.77	26074081
250	Phosphorylation	KKKGKKSSSAEGHTD HCCCCCCCCCCCCHH	42.31	26074081
251	Phosphorylation	KKGKKSSSAEGHTDA CCCCCCCCCCCCHHH	37.11	26074081
256	Phosphorylation	SSSAEGHTDAVLDLS CCCCCCCHHHHHHHH	36.19	26074081
263	Phosphorylation	TDAVLDLSWNKLIRN HHHHHHHHHHHHHHH	28.41	26074081
301	Ubiquitination	SLAVHTDKVQTLQFH EEEECCCCCEEEEEC	37.08	-
327	Phosphorylation	YDKSVALYDCRSPDE CCCCEEEEECCCCCH	11.85	-
331	Phosphorylation	VALYDCRSPDESHRM EEEEECCCCCHHHCH	42.93	29214152
342	Phosphorylation	SHRMWRFSGQIERVT HHCHHEEECEEEEEE	22.63	23312004
394	Phosphorylation	EISGLDLSSQIKGCL CCCCCCHHHCCCCEE	21.62	24719451
403	Phosphorylation	QIKGCLVTASADKYV CCCCEEEECCHHHEE	11.27	28152594
405	Phosphorylation	KGCLVTASADKYVKI CCEEEECCHHHEEEH	27.86	28152594
408	Ubiquitination	LVTASADKYVKIWDI EEECCHHHEEEHHHH	52.22	-
408	Acetylation	LVTASADKYVKIWDI EEECCHHHEEEHHHH	52.22	26051181
409	Phosphorylation	VTASADKYVKIWDIL EECCHHHEEEHHHHH	13.92	28152594
419	Methylation	IWDILGDRPSLVHSR HHHHHCCCCCCCCCC	22.40	115489691
480	Phosphorylation	RERLVLGSARNSSIS CHHEEECCCCCCCCC	21.64	26074081
484	Phosphorylation	VLGSARNSSISGPFG EECCCCCCCCCCCCC	24.40	23927012
485	Phosphorylation	LGSARNSSISGPFGS ECCCCCCCCCCCCCC	25.07	23401153
487	Phosphorylation	SARNSSISGPFGSRS CCCCCCCCCCCCCCC	42.22	23927012
492	Phosphorylation	SISGPFGSRSSDTPM CCCCCCCCCCCCCCC	29.39	23927012
494	Phosphorylation	SGPFGSRSSDTPMES CCCCCCCCCCCCCCC	33.97	25627689
495	Phosphorylation	GPFGSRSSDTPMES- CCCCCCCCCCCCCC-	44.38	25159151
497	Phosphorylation	FGSRSSDTPMES--- CCCCCCCCCCCC---	26.87	23403867
501	Phosphorylation	SSDTPMES------- CCCCCCCC-------	38.99	21406692

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 PWP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PWP1_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 PWP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRP78_HUMAN	HSPA5	physical	20028516
SSBP_HUMAN	SSBP1	physical	20028516
PSG2_HUMAN	PSG2	physical	20028516
A4_HUMAN	APP	physical	21832049
FBRL_HUMAN	FBL	physical	26344197
NOG1_HUMAN	GTPBP4	physical	26344197
PUM3_HUMAN	KIAA0020	physical	26344197
TOP1_HUMAN	TOP1	physical	26344197
ANK3_HUMAN	ANK3	physical	28514442
PP13_HUMAN	LGALS13	physical	28514442
TCAF1_HUMAN	FAM115A	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 PWP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-50; THR-55; SER-57 AND SER-59, AND MASSSPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-50; THR-55; SER-57;SER-59 AND SER-485, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-50; THR-55; SER-57 AND SER-59, AND MASSSPECTROMETRY.	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 SER-50; SER-57 AND SER-59,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 THR-21; SER-50 AND SER-485,AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-65, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-57, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-57, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND MASSSPECTROMETRY.	16565220 [Abstract]