dbPTM

DAZP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DAZP1_HUMAN
UniProt AC	Q96EP5
Protein Name	DAZ-associated protein 1
Gene Name	DAZAP1
Organism	Homo sapiens (Human).
Sequence Length	407
Subcellular Localization	Cytoplasm . Nucleus . Predominantly cytoplasmic (By similarity). Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles.
Protein Description	RNA-binding protein, which may be required during spermatogenesis..
Protein Sequence	MNNSGADEIGKLFVGGLDWSTTQETLRSYFSQYGEVVDCVIMKDKTTNQSRGFGFVKFKDPNCVGTVLASRPHTLDGRNIDPKPCTPRGMQPERTRPKEGWQKGPRSDNSKSNKIFVGGIPHNCGETELREYFKKFGVVTEVVMIYDAEKQRPRGFGFITFEDEQSVDQAVNMHFHDIMGKKVEVKRAEPRDSKSQAPGQPGASQWGSRVVPNAANGWAGQPPPTWQQGYGPQGMWVPAGQAIGGYGPPPAGRGAPPPPPPFTSYIVSTPPGGFPPPQGFPQGYGAPPQFSFGYGPPPPPPDQFAPPGVPPPPATPGAAPLAFPPPPSQAAPDMSKPPTAQPDFPYGQYAGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQGFHPYRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MNNSGADE -------CCCCCHHH	10.92	28183972
1	Acetylation	-------MNNSGADE -------CCCCCHHH	10.92	22223895
4	Phosphorylation	----MNNSGADEIGK ----CCCCCHHHHHH	30.29	22199227
20	Phosphorylation	FVGGLDWSTTQETLR EECCCCCCCCHHHHH	22.65	28857561
21	Phosphorylation	VGGLDWSTTQETLRS ECCCCCCCCHHHHHH	28.39	28857561
22	Phosphorylation	GGLDWSTTQETLRSY CCCCCCCCHHHHHHH	20.92	28857561
39	Glutathionylation	QYGEVVDCVIMKDKT HHCCEEEEEEEECCC	1.19	22555962
43	Ubiquitination	VVDCVIMKDKTTNQS EEEEEEEECCCCCCC	44.97	-
43	Acetylation	VVDCVIMKDKTTNQS EEEEEEEECCCCCCC	44.97	26051181
46	Phosphorylation	CVIMKDKTTNQSRGF EEEEECCCCCCCCCE	40.90	23882029
57 (in isoform 1)	Ubiquitination	-	44.42	21890473
57	2-Hydroxyisobutyrylation	SRGFGFVKFKDPNCV CCCEEEEEECCCCCC	44.42	-
57	Acetylation	SRGFGFVKFKDPNCV CCCEEEEEECCCCCC	44.42	25953088
57 (in isoform 2)	Ubiquitination	-	44.42	21890473
57	Ubiquitination	SRGFGFVKFKDPNCV CCCEEEEEECCCCCC	44.42	21890473
59	Acetylation	GFGFVKFKDPNCVGT CEEEEEECCCCCCEE	67.56	23749302
59	Ubiquitination	GFGFVKFKDPNCVGT CEEEEEECCCCCCEE	67.56	-
59	Malonylation	GFGFVKFKDPNCVGT CEEEEEECCCCCCEE	67.56	26320211
71	Methylation	VGTVLASRPHTLDGR CEEEEECCCCCCCCC	22.78	-
83	2-Hydroxyisobutyrylation	DGRNIDPKPCTPRGM CCCCCCCCCCCCCCC	49.31	-
83	Ubiquitination	DGRNIDPKPCTPRGM CCCCCCCCCCCCCCC	49.31	-
83	Acetylation	DGRNIDPKPCTPRGM CCCCCCCCCCCCCCC	49.31	26822725
86	Phosphorylation	NIDPKPCTPRGMQPE CCCCCCCCCCCCCCC	25.25	25159151
88	Methylation	DPKPCTPRGMQPERT CCCCCCCCCCCCCCC	34.75	-
98	Acetylation	QPERTRPKEGWQKGP CCCCCCCCCCCCCCC	66.62	7681903
98	Ubiquitination	QPERTRPKEGWQKGP CCCCCCCCCCCCCCC	66.62	-
103	Ubiquitination	RPKEGWQKGPRSDNS CCCCCCCCCCCCCCC	65.46	19608861
103	Acetylation	RPKEGWQKGPRSDNS CCCCCCCCCCCCCCC	65.46	19608861
114	Acetylation	SDNSKSNKIFVGGIP CCCCCCCCEEECCCC	44.61	25953088
114	Ubiquitination	SDNSKSNKIFVGGIP CCCCCCCCEEECCCC	44.61	-
124	S-nitrosylation	VGGIPHNCGETELRE ECCCCCCCCHHHHHH	4.78	19483679
124	S-nitrosocysteine	VGGIPHNCGETELRE ECCCCCCCCHHHHHH	4.78	-
134	Ubiquitination	TELREYFKKFGVVTE HHHHHHHHHHCCEEE	46.41	-
150	Acetylation	VMIYDAEKQRPRGFG EEEEEHHHCCCCCEE	54.01	22001406
150	Ubiquitination	VMIYDAEKQRPRGFG EEEEEHHHCCCCCEE	54.01	22001406
194 (in isoform 2)	Ubiquitination	-	51.37	21890473
194 (in isoform 1)	Ubiquitination	-	51.37	21890473
194	Ubiquitination	RAEPRDSKSQAPGQP ECCCCCCCCCCCCCC	51.37	2190698
195	Phosphorylation	AEPRDSKSQAPGQPG CCCCCCCCCCCCCCC	35.21	28555341
204	Phosphorylation	APGQPGASQWGSRVV CCCCCCHHHHCCCCC	32.17	17525332
208	Phosphorylation	PGASQWGSRVVPNAA CCHHHHCCCCCCCCC	20.95	27251275
209	Methylation	GASQWGSRVVPNAAN CHHHHCCCCCCCCCC	29.52	-
253	Methylation	YGPPPAGRGAPPPPP CCCCCCCCCCCCCCC	39.96	24129315
253	Dimethylation	YGPPPAGRGAPPPPP CCCCCCCCCCCCCCC	39.96	-
268	Phosphorylation	PFTSYIVSTPPGGFP CCCEEEEECCCCCCC	26.15	26074081
269	Phosphorylation	FTSYIVSTPPGGFPP CCEEEEECCCCCCCC	23.70	26074081
315	Phosphorylation	GVPPPPATPGAAPLA CCCCCCCCCCCCCCC	28.20	22817900
393	Methylation	AGGSGFGRGQNHNVQ CCCCCCCCCCCCCCC	41.06	-
405	Phosphorylation	NVQGFHPYRR----- CCCCCCCCCC-----	15.50	-

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
269	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
315	T	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
150	K	Acetylation		22001406
Acetylation at Lys-150 is predominantly observed in the nuclear fraction, and may regulate nucleocytoplasmic transport.

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 DAZP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAZL_HUMAN	DAZL	physical	10857750
DAZ1_HUMAN	DAZ1	physical	10857750
ADPPT_HUMAN	AASDHPPT	physical	26344197
ADK_HUMAN	ADK	physical	26344197
AK1A1_HUMAN	AKR1A1	physical	26344197
ARF4_HUMAN	ARF4	physical	26344197
ARF5_HUMAN	ARF5	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
ATOX1_HUMAN	ATOX1	physical	26344197
CHSP1_HUMAN	CARHSP1	physical	26344197
COF1_HUMAN	CFL1	physical	26344197
CRIP1_HUMAN	CRIP1	physical	26344197
DUT_HUMAN	DUT	physical	26344197
DYL1_HUMAN	DYNLL1	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
FUMH_HUMAN	FH	physical	26344197
FUBP3_HUMAN	FUBP3	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
MDHM_HUMAN	MDH2	physical	26344197
MPI_HUMAN	MPI	physical	26344197
MTAP_HUMAN	MTAP	physical	26344197
SIAS_HUMAN	NANS	physical	26344197
NEDD8_HUMAN	NEDD8	physical	26344197
NQO1_HUMAN	NQO1	physical	26344197
PUR6_HUMAN	PAICS	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PROF1_HUMAN	PFN1	physical	26344197
PIN1_HUMAN	PIN1	physical	26344197
PIR_HUMAN	PIR	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
SERC_HUMAN	PSAT1	physical	26344197
RAC1_HUMAN	RAC1	physical	26344197
RBM12_HUMAN	RBM12	physical	26344197
RSU1_HUMAN	RSU1	physical	26344197
SERPH_HUMAN	SERPINH1	physical	26344197
SH3L1_HUMAN	SH3BGRL	physical	26344197
SNX12_HUMAN	SNX12	physical	26344197
SNX3_HUMAN	SNX3	physical	26344197
SODC_HUMAN	SOD1	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
TIA1_HUMAN	TIA1	physical	26344197
TIAR_HUMAN	TIAL1	physical	26344197
TKT_HUMAN	TKT	physical	26344197
TRIA1_HUMAN	TRIAP1	physical	26344197
UB2L3_HUMAN	UBE2L3	physical	26344197

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 DAZP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Acetylation of Prrp K150 regulates the subcellular localization."; Sasaki K., Suzuki A., Kagatsume S., Ono M., Matsuzawa K., Taguchi Y.,Kurihara Y.; Gene 491:13-19(2012). Cited for: ACETYLATION AT LYS-150, AND SUBCELLULAR LOCATION.	22001406 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND MASSSPECTROMETRY.	17525332 [Abstract]

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