dbPTM

APLF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APLF_HUMAN
UniProt AC	Q8IW19
Protein Name	Aprataxin and PNK-like factor
Gene Name	APLF
Organism	Homo sapiens (Human).
Sequence Length	511
Subcellular Localization	Nucleus. Cytoplasm, cytosol. Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers.
Protein Description	Nuclease involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage..
Protein Sequence	MSGGFELQPRDGGPRVALAPGETVIGRGPLLGITDKRVSRRHAILEVAGGQLRIKPIHTNPCFYQSSEKSQLLPLKPNLWCYLNPGDSFSLLVDKYIFRILSIPSEVEMQCTLRNSQVLDEDNILNETPKSPVINLPHETTGASQLEGSTEIAKTQMTPTNSVSFLGENRDCNKQQPILAERKRILPTWMLAEHLSDQNLSVPAISGGNVIQGSGKEEICKDKSQLNTTQQGRRQLISSGSSENTSAEQDTGEECKNTDQEESTISSKEMPQSFSAITLSNTEMNNIKTNAQRNKLPIEELGKVSKHKIATKRTPHKEDEAMSCSENCSSAQGDSLQDESQGSHSESSSNPSNPETLHAKATDSVLQGSEGNKVKRTSCMYGANCYRKNPVHFQHFSHPGDSDYGGVQIVGQDETDDRPECPYGPSCYRKNPQHKIEYRHNTLPVRNVLDEDNDNVGQPNEYDLNDSFLDDEEEDYEPTDEDSDWEPGKEDEEKEDVEELLKEAKRFMKRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
116	Phosphorylation	MQCTLRNSQVLDEDN EEEEECCCCCCCCCC	18.42	17507382
128	Phosphorylation	EDNILNETPKSPVIN CCCCCCCCCCCCCCC	34.64	28450419
131	Phosphorylation	ILNETPKSPVINLPH CCCCCCCCCCCCCCC	26.13	29255136
140	Phosphorylation	VINLPHETTGASQLE CCCCCCCCCCCHHCC	27.74	28450419
141	Phosphorylation	INLPHETTGASQLEG CCCCCCCCCCHHCCC	27.97	26657352
144	Phosphorylation	PHETTGASQLEGSTE CCCCCCCHHCCCCCE	36.32	28450419
149	Phosphorylation	GASQLEGSTEIAKTQ CCHHCCCCCEEECCC	17.31	28450419
150	Phosphorylation	ASQLEGSTEIAKTQM CHHCCCCCEEECCCC	42.12	28450419
155	Phosphorylation	GSTEIAKTQMTPTNS CCCEEECCCCCCCCC	17.98	28857561
158	Phosphorylation	EIAKTQMTPTNSVSF EEECCCCCCCCCEEE	19.69	28857561
160	Phosphorylation	AKTQMTPTNSVSFLG ECCCCCCCCCEEECC	30.84	22210691
239	Phosphorylation	GRRQLISSGSSENTS HHHHHHHCCCCCCCC	35.38	28348404
241	Phosphorylation	RQLISSGSSENTSAE HHHHHCCCCCCCCCC	36.10	28348404
242	Phosphorylation	QLISSGSSENTSAEQ HHHHCCCCCCCCCCC	38.09	28348404
245	Phosphorylation	SSGSSENTSAEQDTG HCCCCCCCCCCCCCC	25.84	28348404
246	Phosphorylation	SGSSENTSAEQDTGE CCCCCCCCCCCCCCH	41.19	28348404
263	Phosphorylation	KNTDQEESTISSKEM CCCCHHHCCCCCCCC	30.23	30576142
377	Phosphorylation	EGNKVKRTSCMYGAN CCCCCCCCCCCCCCC	22.14	24114839
378	Phosphorylation	GNKVKRTSCMYGANC CCCCCCCCCCCCCCC	10.83	24114839
381	Phosphorylation	VKRTSCMYGANCYRK CCCCCCCCCCCCCCC	19.88	24114839
386	Phosphorylation	CMYGANCYRKNPVHF CCCCCCCCCCCCCCE	25.16	24114839

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
116	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
H31T_HUMAN	HIST3H3	physical	21211722
PARP1_HUMAN	PARP1	physical	17396150
PARP1_HUMAN	PARP1	physical	20098424
A4_HUMAN	APP	physical	21832049
H2AW_HUMAN	H2AFY2	physical	26186194
H2AY_HUMAN	H2AFY	physical	26186194
SP16H_HUMAN	SUPT16H	physical	26186194
XRCC1_HUMAN	XRCC1	physical	26186194
DNLI3_HUMAN	LIG3	physical	26186194
PARP2_HUMAN	PARP2	physical	26186194
PARP1_HUMAN	PARP1	physical	26186194
XRCC6_HUMAN	XRCC6	physical	26186194
HLTF_HUMAN	HLTF	physical	26186194
XRCC5_HUMAN	XRCC5	physical	26186194
H2B1J_HUMAN	HIST1H2BJ	physical	26186194
DNLI4_HUMAN	LIG4	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
XRCC4_HUMAN	XRCC4	physical	26186194
CHD1L_HUMAN	CHD1L	physical	26186194
XPC_HUMAN	XPC	physical	26186194
CETN2_HUMAN	CETN2	physical	26186194
TYDP1_HUMAN	TDP1	physical	26186194
TOP1_HUMAN	TOP1	physical	26186194
SSRP1_HUMAN	SSRP1	physical	26186194
ZG16B_HUMAN	ZG16B	physical	26186194
CYTS_HUMAN	CST4	physical	26186194
PARP1_HUMAN	PARP1	physical	27067600
H2A2C_HUMAN	HIST2H2AC	physical	27067600
H2AY_HUMAN	H2AFY	physical	27067600
H31T_HUMAN	HIST3H3	physical	27067600
XRCC6_HUMAN	XRCC6	physical	27067600
XRCC1_HUMAN	XRCC1	physical	27067600
XRCC6_HUMAN	XRCC6	physical	28514442
DNLI3_HUMAN	LIG3	physical	28514442
XRCC1_HUMAN	XRCC1	physical	28514442
XPC_HUMAN	XPC	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
H2AW_HUMAN	H2AFY2	physical	28514442
DNLI4_HUMAN	LIG4	physical	28514442
TYDP1_HUMAN	TDP1	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442
MSH3_HUMAN	MSH3	physical	28514442
XRCC4_HUMAN	XRCC4	physical	28514442
XRCC5_HUMAN	XRCC5	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
CYTN_HUMAN	CST1	physical	28514442
HLTF_HUMAN	HLTF	physical	28514442
SSRP1_HUMAN	SSRP1	physical	28514442
CYTS_HUMAN	CST4	physical	28514442
CHD1L_HUMAN	CHD1L	physical	28514442
ZG16B_HUMAN	ZG16B	physical	28514442
CETN2_HUMAN	CETN2	physical	28514442
H2A2B_HUMAN	HIST2H2AB	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 APLF_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Human Xip1 (C2orf13) is a novel regulator of cellular responses toDNA strand breaks."; Bekker-Jensen S., Fugger K., Danielsen J.R., Gromova I., Sehested M.,Celis J., Bartek J., Lukas J., Mailand N.; J. Biol. Chem. 282:19638-19643(2007). Cited for: SUBCELLULAR LOCATION, INTERACTION WITH XRCC1, PHOSPHORYLATION ATSER-116, AND MUTAGENESIS OF SER-116.	17507382 [Abstract]