dbPTM

FA83G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FA83G_HUMAN
UniProt AC	A6ND36
Protein Name	Protein FAM83G
Gene Name	FAM83G
Organism	Homo sapiens (Human).
Sequence Length	823
Subcellular Localization	Cytoplasm, cytosol . Nucleus . Detected predominantly in cytosolic. Upon BMP stimulation, a small portion of PAWS1 is detected in the nucleus.
Protein Description	May regulate the bone morphogenetic proteins (BMP) pathway..
Protein Sequence	MAFSQVQCLDDNHVNWRSSESKPEFFYSEEQRLALEALVARGRDAFYEVLKRENIRDFLSELELKRILETIEVYDPGSEDPRGTGPSQGPEDNGVGDGEEASGADGVPIEAEPLPSLEYWPQKSDRSIPQLDLGWPDTIAYRGVTRASVYMQPPIDGQAHIKEVVRKMISQAQKVIAVVMDMFTDVDIFKDLLDAGFKRKVAVYIIVDESNVKYFLHMCERACMHLGHLKNLRVRSSGGTEFFTRSATKFKGALAQKFMFVDGDRAVCGSYSFTWSAARTDRNVISVLSGQVVEMFDRQFQELYLMSHSVSLKGIPMEKEPEPEPIVLPSVVPLVPAGTVAKKLVNPKYALVKAKSVDEIAKISSEKQEAKKPLGLKGPALAEHPGELPELLPPIHPGLLHLERANMFEYLPTWVEPDPEPGSDILGYINIIDPNIWNPQPSQMNRIKIRDTSQASAQHQLWKQSQDSRPRPEPCPPPEPSAPQDGVPAENGLPQGDPEPLPPVPKPRTVPVADVLARDSSDIGWVLELPKEEAPQNGTDHRLPRMAGPGHAPLQRQLSVTQDDPESLGVGLPNGLDGVEEEDDDDYVTLSDQDSHSGSSGRGPGPRRPSVASSVSEEYFEVREHSVPLRRRHSEQVANGPTPPPRRQLSAPHITRGTFVGPQGGSPWAQSRGREEADALKRMQAQRSTDKEAQGQQFHHHRVPASGTRDKDGFPGPPRYRSAADSVQSSTRNAGPAMAGPHHWQAKGGQVPRLLPDPGSPRLAQNARPMTDGRATEEHPSPFGIPYSKLSQSKHLKARTGGSQWASSDSKRRAQAPRDRKDP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAFSQVQCL ------CCCCCEEEC	16.88	21406692
4	Phosphorylation	----MAFSQVQCLDD ----CCCCCEEECCC	21.65	23401153
18	Phosphorylation	DNHVNWRSSESKPEF CCCCCCCCCCCCCCC	30.03	23312004
19	Phosphorylation	NHVNWRSSESKPEFF CCCCCCCCCCCCCCC	37.00	23312004
21	Phosphorylation	VNWRSSESKPEFFYS CCCCCCCCCCCCCCC	56.30	23312004
22	Ubiquitination	NWRSSESKPEFFYSE CCCCCCCCCCCCCCH	44.51	29967540
27	Phosphorylation	ESKPEFFYSEEQRLA CCCCCCCCCHHHHHH	22.09	23312004
28	Phosphorylation	SKPEFFYSEEQRLAL CCCCCCCCHHHHHHH	29.51	23312004
51	Ubiquitination	DAFYEVLKRENIRDF HHHHHHHHHCCHHHH	63.94	29967540
65	Ubiquitination	FLSELELKRILETIE HHHHHHHHHHHHHEE	28.19	29967540
116	Phosphorylation	IEAEPLPSLEYWPQK CCCEECCCCCCCCCC	41.33	26471730
119	Phosphorylation	EPLPSLEYWPQKSDR EECCCCCCCCCCCCC	27.90	26471730
124	Phosphorylation	LEYWPQKSDRSIPQL CCCCCCCCCCCCCCC	32.77	22617229
127	Phosphorylation	WPQKSDRSIPQLDLG CCCCCCCCCCCCCCC	43.54	30266825
138	Phosphorylation	LDLGWPDTIAYRGVT CCCCCCCCEEECCCC	11.92	27251275
141	Phosphorylation	GWPDTIAYRGVTRAS CCCCCEEECCCCEEE	12.21	23090842
148	Phosphorylation	YRGVTRASVYMQPPI ECCCCEEEEEECCCC	15.53	28555341
198	Acetylation	DLLDAGFKRKVAVYI HHHHHCCCCCEEEEE	50.85	30588715
210	Phosphorylation	VYIIVDESNVKYFLH EEEEECCCHHHHHHH	42.32	-
251	Methylation	TRSATKFKGALAQKF ECCHHHCCCCCCCCE	44.84	-
270	Phosphorylation	GDRAVCGSYSFTWSA CCEEECEEEEEEEEE	16.69	28258704
276	Phosphorylation	GSYSFTWSAARTDRN EEEEEEEEECCCCCC	14.70	28258704
304	Phosphorylation	DRQFQELYLMSHSVS HHHHHHHHHHHCCCC	10.29	-
356	Phosphorylation	YALVKAKSVDEIAKI HHEEEECCHHHHHHH	39.39	23401153
364	Phosphorylation	VDEIAKISSEKQEAK HHHHHHHCHHHHHHC	31.57	23312004
365	Phosphorylation	DEIAKISSEKQEAKK HHHHHHCHHHHHHCC	52.89	26657352
452	Phosphorylation	NRIKIRDTSQASAQH CCEEECCCCHHHHHH	16.94	27251275
453	Phosphorylation	RIKIRDTSQASAQHQ CEEECCCCHHHHHHH	28.21	27282143
456	Phosphorylation	IRDTSQASAQHQLWK ECCCCHHHHHHHHHH	22.33	28348404
463	Methylation	SAQHQLWKQSQDSRP HHHHHHHHHCCCCCC	48.98	-
509	Phosphorylation	PPVPKPRTVPVADVL CCCCCCCCCCHHHHC	37.37	28555341
520	Phosphorylation	ADVLARDSSDIGWVL HHHCCCCCCCCEEEE	25.10	28348404
521	Phosphorylation	DVLARDSSDIGWVLE HHCCCCCCCCEEEEE	37.22	28348404
559	Phosphorylation	APLQRQLSVTQDDPE CCHHHCCEECCCCHH	18.12	-
561	Phosphorylation	LQRQLSVTQDDPESL HHHCCEECCCCHHHC	23.93	30576142
591	Phosphorylation	DDDYVTLSDQDSHSG CCCCEECCCCCCCCC	24.70	30576142
599	Phosphorylation	DQDSHSGSSGRGPGP CCCCCCCCCCCCCCC	32.41	30576142
610	Phosphorylation	GPGPRRPSVASSVSE CCCCCCCCCCCHHCH	28.62	21712546
613	Phosphorylation	PRRPSVASSVSEEYF CCCCCCCCHHCHHHH	29.17	21712546
614	Phosphorylation	RRPSVASSVSEEYFE CCCCCCCHHCHHHHH	21.67	21712546
616	Phosphorylation	PSVASSVSEEYFEVR CCCCCHHCHHHHHHH	27.02	24554596
619	Phosphorylation	ASSVSEEYFEVREHS CCHHCHHHHHHHCCC	10.86	20873877
634	Phosphorylation	VPLRRRHSEQVANGP CCCCHHCHHHHHCCC	28.10	30266825
642	Phosphorylation	EQVANGPTPPPRRQL HHHHCCCCCCCCHHC	50.23	29496963
650	Phosphorylation	PPPRRQLSAPHITRG CCCCHHCCCCCCCCC	31.26	30266825
655	Phosphorylation	QLSAPHITRGTFVGP HCCCCCCCCCCEECC	21.73	30266825
658	Phosphorylation	APHITRGTFVGPQGG CCCCCCCCEECCCCC	16.32	27732954
666	Phosphorylation	FVGPQGGSPWAQSRG EECCCCCCHHHHHCC	24.88	25159151
671	Phosphorylation	GGSPWAQSRGREEAD CCCHHHHHCCHHHHH	29.02	27732954
688	Phosphorylation	KRMQAQRSTDKEAQG HHHHHHHCCCHHHHH	28.95	26657352
689	Phosphorylation	RMQAQRSTDKEAQGQ HHHHHHCCCHHHHHH	53.96	26657352
720	Phosphorylation	GFPGPPRYRSAADSV CCCCCCCCCHHHHHH	18.07	23312004
722	Phosphorylation	PGPPRYRSAADSVQS CCCCCCCHHHHHHHH	20.90	24719451
726	Phosphorylation	RYRSAADSVQSSTRN CCCHHHHHHHHHCCC	19.82	25332170
729	Phosphorylation	SAADSVQSSTRNAGP HHHHHHHHHCCCCCC	31.36	25332170
747	Methylation	GPHHWQAKGGQVPRL CCCCHHCCCCCCCCC	48.77	-
760	Phosphorylation	RLLPDPGSPRLAQNA CCCCCCCCCHHHHCC	16.54	25159151
776	Phosphorylation	PMTDGRATEEHPSPF CCCCCCCCCCCCCCC	40.31	22199227
781	Phosphorylation	RATEEHPSPFGIPYS CCCCCCCCCCCCCHH	34.47	22199227
788	Phosphorylation	SPFGIPYSKLSQSKH CCCCCCHHHHCCCCC	23.05	28348404
791	Phosphorylation	GIPYSKLSQSKHLKA CCCHHHHCCCCCCCH	35.82	28348404
793	Phosphorylation	PYSKLSQSKHLKART CHHHHCCCCCCCHHC	20.75	24719451
807	Phosphorylation	TGGSQWASSDSKRRA CCCCCCCCCHHHHHH	31.55	24719451
810	Phosphorylation	SQWASSDSKRRAQAP CCCCCCHHHHHHCCC	29.97	-

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
356	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
610	S	Phosphorylation	24554596
BMP signaling induces the phosphorylation of PAWS1 by BMPR1A at Ser-610, Ser-614 and Ser-616.
610	S	Phosphorylation	24554596
In response to BMP phosphorylation at Ser-610 is necessary for the activation of SMAD4-independent BMP target genes such as NEDD9 and ASNS.
614	S	Phosphorylation	24554596
BMP signaling induces the phosphorylation of PAWS1 by BMPR1A at Ser-610, Ser-614 and Ser-616.
616	S	Phosphorylation	24554596
BMP signaling induces the phosphorylation of PAWS1 by BMPR1A at Ser-610, Ser-614 and Ser-616.

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 FA83G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of FA83G_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.

Regulatory Network of FA83G_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-356 AND SER-666, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASSSPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASSSPECTROMETRY.	16964243 [Abstract]

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