PAF15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAF15_HUMAN
• UniProt AC: Q15004
• Protein Name: PCNA-associated factor {ECO:0000305}
• Gene Name: PCLAF {ECO:0000312|HGNC:HGNC:28961}
• Organism: Homo sapiens (Human).
• Sequence Length: 111
• Subcellular Localization: Nucleus . Cytoplasm, perinuclear region . Following DNA damage, localizes to DNA damage sites (PubMed:21628590). Colocalizes with centrosomes in perinuclear region (PubMed:21673012).
• Protein Description: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number..
• Protein Sequence: MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRKACPLQPDHTNDEKE

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
4	Phosphorylation	----MVRTKADSVPG ----CCCCCCCCCCC		23186163
5	Ubiquitination	---MVRTKADSVPGT ---CCCCCCCCCCCC		33845483
8	Phosphorylation	MVRTKADSVPGTYRK CCCCCCCCCCCCHHH		25159151
12	Phosphorylation	KADSVPGTYRKVVAA CCCCCCCCHHHHHHH		21552520
13	Phosphorylation	ADSVPGTYRKVVAAR CCCCCCCHHHHHHHC		29396449
15	Methylation	SVPGTYRKVVAARAP CCCCCHHHHHHHCCC		-
15	Ubiquitination	SVPGTYRKVVAARAP CCCCCHHHHHHHCCC		21906983
24 (in isoform 2)	Ubiquitination	-		20972266
24	Ubiquitination	VAARAPRKVLGSSTS HHHCCCCEECCCCCC		21890473
24	Neddylation	VAARAPRKVLGSSTS HHHCCCCEECCCCCC		32015554
24	Acetylation	VAARAPRKVLGSSTS HHHCCCCEECCCCCC		-
24	Ubiquitination	VAARAPRKVLGSSTS HHHCCCCEECCCCCC		23000965
28	Phosphorylation	APRKVLGSSTSATNS CCCEECCCCCCCCCC		30206219
29	Phosphorylation	PRKVLGSSTSATNST CCEECCCCCCCCCCC		20068231
30	Phosphorylation	RKVLGSSTSATNSTS CEECCCCCCCCCCCC		25159151
31	Phosphorylation	KVLGSSTSATNSTSV EECCCCCCCCCCCCC		25159151
33	Phosphorylation	LGSSTSATNSTSVSS CCCCCCCCCCCCCCC		25850435
35 (in isoform 2)	Phosphorylation	-		29507054
35	Phosphorylation	SSTSATNSTSVSSRK CCCCCCCCCCCCCCH		25850435
36	Phosphorylation	STSATNSTSVSSRKA CCCCCCCCCCCCCHH		25850435
37	Phosphorylation	TSATNSTSVSSRKAE CCCCCCCCCCCCHHC		25850435
39	Phosphorylation	ATNSTSVSSRKAENK CCCCCCCCCCHHCCC		20068231
39 (in isoform 2)	Phosphorylation	-		29507054
40	Phosphorylation	TNSTSVSSRKAENKY CCCCCCCCCHHCCCC		20068231
46	Ubiquitination	SSRKAENKYAGGNPV CCCHHCCCCCCCCCE		29967540
47	Phosphorylation	SRKAENKYAGGNPVC CCHHCCCCCCCCCEE		28152594
58	Phosphorylation	NPVCVRPTPKWQKGI CCEEECCCHHHHCCC		28555341
60	Ubiquitination	VCVRPTPKWQKGIGE EEECCCHHHHCCCHH		29967540
63	Ubiquitination	RPTPKWQKGIGEFFR CCCHHHHCCCHHHHC		21906983
72	Phosphorylation	IGEFFRLSPKDSEKE CHHHHCCCCCCHHHH		30266825
76	Phosphorylation	FRLSPKDSEKENQIP HCCCCCCHHHHHCCC		26074081
78	Ubiquitination	LSPKDSEKENQIPEE CCCCCHHHHHCCCHH		33845483
78	Acetylation	LSPKDSEKENQIPEE CCCCCHHHHHCCCHH		26051181
88	Phosphorylation	QIPEEAGSSGLGKAK CCCHHHHCCCCCHHH		21815630
89	Phosphorylation	IPEEAGSSGLGKAKR CCHHHHCCCCCHHHH		28985074
93	Acetylation	AGSSGLGKAKRKACP HHCCCCCHHHHHCCC		25953088
93	Ubiquitination	AGSSGLGKAKRKACP HHCCCCCHHHHHCCC		33845483
95	Acetylation	SSGLGKAKRKACPLQ CCCCCHHHHHCCCCC		20167786
97	Ubiquitination	GLGKAKRKACPLQPD CCCHHHHHCCCCCCC		33845483
106	Phosphorylation	CPLQPDHTNDEKE-- CCCCCCCCCCCCC--		30266825
110	Acetylation	PDHTNDEKE------ CCCCCCCCC------		26822725

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
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:21700221

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
15	K	ubiquitylation	Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24 are probably extended, leading to disrupt the interaction with PCNA.	23000965
15	K	ubiquitylation	Monoubiquitinated at Lys-15 and Lys-24 during normal S phase, promoting its association with PCNA.	23000965
24	K	ubiquitylation	Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24 are probably extended, leading to disrupt the interaction with PCNA.	23000965
24	K	ubiquitylation	Monoubiquitinated at Lys-15 and Lys-24 during normal S phase, promoting its association with PCNA.	23000965

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PAF15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCNA_HUMAN	PCNA	physical	11313979
ICAL_HUMAN	CAST	physical	21263028
ING1_HUMAN	ING1	physical	16288740
PCNA_HUMAN	PCNA	physical	16288740
DNMT1_HUMAN	DNMT1	physical	21628590
BUD31_HUMAN	BUD31	physical	21628590
PARG_HUMAN	PARG	physical	21628590
YTDC1_HUMAN	YTHDC1	physical	21628590
ZC11A_HUMAN	ZC3H11A	physical	21628590
ZCCHL_HUMAN	ZC3HAV1L	physical	21628590
NUMA1_HUMAN	NUMA1	physical	21628590
RRBP1_HUMAN	RRBP1	physical	21628590
TPR_HUMAN	TPR	physical	21628590
SPTB2_HUMAN	SPTBN1	physical	21628590
PININ_HUMAN	PNN	physical	21628590
ODP2_HUMAN	DLAT	physical	21628590
PCNA_HUMAN	PCNA	physical	21628590
ANFY1_HUMAN	ANKFY1	physical	21628590
SNUT1_HUMAN	SART1	physical	21628590
HECD1_HUMAN	HECTD1	physical	22863883
SYHC_HUMAN	HARS	physical	26344197
HSP7E_HUMAN	HSPA14	physical	26344197
PCNA_HUMAN	PCNA	physical	21700221
FZR1_HUMAN	FZR1	physical	21700221

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.