PAPS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAPS2_HUMAN
• UniProt AC: O95340
• Protein Name: Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
• Gene Name: PAPSS2
• Organism: Homo sapiens (Human).
• Sequence Length: 614
• Protein Description: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. May have a important role in skeletogenesis during postnatal growth (By similarity)..
• Protein Sequence: MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLEKN

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
5	Acetylation	---MSGIKKQKTENQ ---CCCCCCCCCCCC	53.31	-
9	Phosphorylation	SGIKKQKTENQQKST CCCCCCCCCCCHHHC	37.36	20068231
15	Phosphorylation	KTENQQKSTNVVYQA CCCCCHHHCCCEEEE	22.37	28152594
16	Phosphorylation	TENQQKSTNVVYQAH CCCCHHHCCCEEEEE	38.78	28152594
20	Phosphorylation	QKSTNVVYQAHHVSR HHHCCCEEEEEECCC	8.83	25159151
20 (in isoform 2)	Phosphorylation	-	8.83	27642862
26	Phosphorylation	VYQAHHVSRNKRGQV EEEEEECCCCCCCCE	26.27	28152594
37	Methylation	RGQVVGTRGGFRGCT CCCEEECCCCCCCCE	36.99	-
92	Phosphorylation	LNRNLGFSPGDREEN CCCCCCCCCCCHHHH	26.61	21815630
92 (in isoform 2)	Phosphorylation	-	26.61	27251275
173 (in isoform 2)	Ubiquitination	-	43.60	21890473
173	Ubiquitination	RARAGEIKGFTGIDS HHHHCCCCCCCCCCC	43.60	-
173 (in isoform 1)	Ubiquitination	-	43.60	21890473
173	Malonylation	RARAGEIKGFTGIDS HHHHCCCCCCCCCCC	43.60	26320211
180 (in isoform 2)	Phosphorylation	-	39.92	27642862
180	Phosphorylation	KGFTGIDSDYEKPET CCCCCCCCCCCCCCC	39.92	25159151
182	Phosphorylation	FTGIDSDYEKPETPE CCCCCCCCCCCCCHH	29.79	26270265
182 (in isoform 2)	Phosphorylation	-	29.79	27642862
184 (in isoform 2)	Ubiquitination	-	41.76	21890473
184 (in isoform 1)	Ubiquitination	-	41.76	21890473
184	Acetylation	GIDSDYEKPETPERV CCCCCCCCCCCHHHH	41.76	26051181
184	Ubiquitination	GIDSDYEKPETPERV CCCCCCCCCCCHHHH	41.76	21906983
187 (in isoform 2)	Phosphorylation	-	38.69	27251275
187	Phosphorylation	SDYEKPETPERVLKT CCCCCCCCHHHHHHH	38.69	29496963
233	Malonylation	ELFVPENKLDHVRAE HHCCCCHHCHHHHHC	54.34	26320211
233	Ubiquitination	ELFVPENKLDHVRAE HHCCCCHHCHHHHHC	54.34	-
248	Phosphorylation	AETLPSLSITKLDLQ HHCCCCCCEEEECCH	32.33	24719451
315	Acetylation	TRLEGCSKFVLAHGG HHCCCCCEEEEEECC	43.50	26051181
349	Phosphorylation	CSRVWGTTCTKHPHI HHCCCCCCCCCCCCE	17.78	-
351	Phosphorylation	RVWGTTCTKHPHIKM CCCCCCCCCCCCEEE	30.23	-
352	Ubiquitination	VWGTTCTKHPHIKMV CCCCCCCCCCCEEEE	58.23	-
394	Ubiquitination	RLTPLELKQKCKEMN CCCHHHHHHHHHHCC	38.03	-
435	Malonylation	RLLERGYKHPVLLLH HHHHCCCCCCEEEEE	44.23	26320211
449	Ubiquitination	HPLGGWTKDDDVPLD EECCCCCCCCCCCCC	53.29	-
460	Ubiquitination	VPLDWRMKQHAAVLE CCCCHHHHHHHHHHH	30.29	-
508	Phosphorylation	MIAGANFYIVGRDPA EECCCCEEEEECCCC	8.43	20860994
517	Sulfoxidation	VGRDPAGMPHPETKK EECCCCCCCCCCCCC	2.75	30846556
522	Phosphorylation	AGMPHPETKKDLYEP CCCCCCCCCCCCCCC	48.09	20860994
534	Ubiquitination	YEPTHGGKVLSMAPG CCCCCCCEEEECCCC	44.59	-
538	Sulfoxidation	HGGKVLSMAPGLTSV CCCEEEECCCCCCEE	4.57	30846556
562	Sulfoxidation	YNKAKKAMDFYDPAR HHHHHHHHHCCCHHH	5.13	30846556
565	Phosphorylation	AKKAMDFYDPARHNE HHHHHHCCCHHHCCC	19.43	29438985
577	Phosphorylation	HNEFDFISGTRMRKL CCCCCCCCCHHHHHH	33.82	25849741
579	Phosphorylation	EFDFISGTRMRKLAR CCCCCCCHHHHHHHH	17.94	25849741
582 (in isoform 2)	Phosphorylation	-	27.78	27251275
596	Sulfoxidation	ENPPDGFMAPKAWKV CCCCCCCCCHHHHHH	8.36	30846556
599 (in isoform 1)	Ubiquitination	-	58.29	21890473
599	Ubiquitination	PDGFMAPKAWKVLTD CCCCCCHHHHHHHHH	58.29	21890473
602	Ubiquitination	FMAPKAWKVLTDYYR CCCHHHHHHHHHHHH	32.02	2189047
602 (in isoform 1)	Ubiquitination	-	32.02	21890473
604 (in isoform 2)	Ubiquitination	-	2.40	21890473
607 (in isoform 2)	Ubiquitination	-	8.78	21890473
610	Phosphorylation	VLTDYYRSLEKN--- HHHHHHHHHHCC---	25.43	29514088

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

Oops, there are no upstream regulatory protein records of PAPS2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAPS2_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 PAPS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
APEX1_HUMAN	APEX1	physical	22863883
ARI2_HUMAN	ARIH2	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
RIC8A_HUMAN	RIC8A	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
TRXR1_HUMAN	TXNRD1	physical	22863883

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612847: Brachyolmia type 4 with mild epiphyseal and metaphyseal changes (BCYM4)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.