PA1B2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PA1B2_HUMAN
• UniProt AC: P68402
• Protein Name: Platelet-activating factor acetylhydrolase IB subunit beta
• Gene Name: PAFAH1B2
• Organism: Homo sapiens (Human).
• Sequence Length: 229
• Subcellular Localization: Cytoplasm.
• Protein Description: Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit..
• Protein Sequence: MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA

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
2	Phosphorylation	------MSQGDSNPA ------CCCCCCCCC	42.76	29255136
2	Acetylation	------MSQGDSNPA ------CCCCCCCCC	42.76	19413330
6	Phosphorylation	--MSQGDSNPAAIPH --CCCCCCCCCCCCC	52.08	30266825
26	Phosphorylation	QGDDRWMSQHNRFVL CCCCCHHHHCCCEEE	22.71	22115753
36	Ubiquitination	NRFVLDCKDKEPDVL CCEEEECCCCCCCEE	72.07	-
48	Phosphorylation	DVLFVGDSMVQLMQQ CEEEECHHHHHHHHH	18.22	30257219
56	Phosphorylation	MVQLMQQYEIWRELF HHHHHHHHHHHHHHH	7.78	30257219
64	Phosphorylation	EIWRELFSPLHALNF HHHHHHHCHHHHHCC	38.89	29255136
86	Ubiquitination	RHVLWRLKNGELENI HHHHHHCCCCCCCCC	55.09	-
133	Ubiquitination	NTRQPQAKIIVLGLL HCCCCCCEEEEEECC	27.93	21890473
133	Ubiquitination	NTRQPQAKIIVLGLL HCCCCCCEEEEEECC	27.93	21890473
145	Ubiquitination	GLLPRGEKPNPLRQK ECCCCCCCCCCHHHH	53.58	-
145 (in isoform 4)	Phosphorylation	-	53.58	-
145	Acetylation	GLLPRGEKPNPLRQK ECCCCCCCCCCHHHH	53.58	25953088
155	Ubiquitination	PLRQKNAKVNQLLKV CHHHHCHHHHHHHHH	51.62	-
155	Acetylation	PLRQKNAKVNQLLKV CHHHHCHHHHHHHHH	51.62	25953088
161	Ubiquitination	AKVNQLLKVSLPKLA HHHHHHHHHHCCHHC	38.07	-
161	Acetylation	AKVNQLLKVSLPKLA HHHHHHHHHHCCHHC	38.07	25953088
163	Phosphorylation	VNQLLKVSLPKLANV HHHHHHHHCCHHCCC	37.05	30576142
207	Ubiquitination	GGYAKICKPLHELIM CHHHHHCHHHHHHHH	54.83	2063986
220	Phosphorylation	IMQLLEETPEEKQTT HHHHHHHCHHHHHCC	26.99	22199227
224	Sumoylation	LEETPEEKQTTIA-- HHHCHHHHHCCCC--	51.81	-

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

Oops, there are no upstream regulatory protein records of PA1B2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PA1B2_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 PA1B2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PA1B3_HUMAN	PAFAH1B3	physical	16189514
ACINU_HUMAN	ACIN1	physical	16169070
TCPG_HUMAN	CCT3	physical	16169070
PINX1_HUMAN	PINX1	physical	16169070
PP12C_HUMAN	PPP1R12C	physical	16169070
REXO1_HUMAN	REXO1	physical	16169070
TIM50_HUMAN	TIMM50	physical	16169070
TISB_HUMAN	ZFP36L1	physical	16169070
PRKN_HUMAN	PARK2	physical	16169070
RLA0_HUMAN	RPLP0	physical	16169070
LIS1_HUMAN	PAFAH1B1	physical	10727864
PSF3_HUMAN	GINS3	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
LDHB_HUMAN	LDHB	physical	22863883
ULA1_HUMAN	NAE1	physical	22863883
CN166_HUMAN	C14orf166	physical	26344197
FA98B_HUMAN	FAM98B	physical	26344197
PSMG1_HUMAN	PSMG1	physical	26344197
RTCB_HUMAN	RTCB	physical	26344197
GLYM_HUMAN	SHMT2	physical	26344197
SYVC_HUMAN	VARS	physical	26344197
WDR4_HUMAN	WDR4	physical	26344197
NDEL1_HUMAN	NDEL1	physical	27173435

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-2, AND MASSSPECTROMETRY.
PubMed: 19413330