ZP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZP3_HUMAN
• UniProt AC: P21754
• Protein Name: Zona pellucida sperm-binding protein 3
• Gene Name: ZP3
• Organism: Homo sapiens (Human).
• Sequence Length: 424
• Subcellular Localization: Processed zona pellucida sperm-binding protein 3: Secreted, extracellular space, extracellular matrix . The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida.; Cell membrane ; Single-pass
• Protein Description: The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation..
• Protein Sequence: MELSYRLFICLLLWGSTELCYPQPLWLLQGGASHPETSVQPVLVECQEATLMVMVSKDLFGTGKLIRAADLTLGPEACEPLVSMDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIECRYPRQGNVSSQAILPTWLPFRTTVFSEEKLTFSLRLMEENWNAEKRSPTFHLGDAAHLQAEIHTGSHVPLRLFVDHCVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFKVPRPGPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKPSNSWFPVEGSADICQCCNKGDCGTPSHSRRQPHVMSQWSRSASRNRRHVTEEADVTVGPLIFLDRRGDHEVEQWALPSDTSVVLLGVGLAVVVSLTLTAVILVLTRRCRTASHPVSASE

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
23	Pyrrolidone_carboxylic_acid	STELCYPQPLWLLQG CCCCCCCCCEEEECC	21.17	-
23	Pyrrolidone_carboxylic_acid	STELCYPQPLWLLQG CCCCCCCCCEEEECC	21.17	15379548
23	Pyrrolidone_carboxylic_acid	STELCYPQPLWLLQG CCCCCCCCCEEEECC	21.17	15379548
64	Ubiquitination	KDLFGTGKLIRAADL CCCCCCCCEEEHHCC	40.35	33845483
125	N-linked_Glycosylation	HDPRPVGNLSIVRTN CCCCCCCCEEEEECC	30.74	15379548
127	Phosphorylation	PRPVGNLSIVRTNRA CCCCCCEEEEECCCC	24.04	24719451
147	N-linked_Glycosylation	CRYPRQGNVSSQAIL ECCCCCCCCCCCEEC	23.35	15379548
149	Phosphorylation	YPRQGNVSSQAILPT CCCCCCCCCCEECCC	22.26	-
150	Phosphorylation	PRQGNVSSQAILPTW CCCCCCCCCEECCCC	21.24	-
156	O-linked_Glycosylation	SSQAILPTWLPFRTT CCCEECCCCCCCCEE	35.87	UniProtKB CARBOHYD
162	O-linked_Glycosylation	PTWLPFRTTVFSEEK CCCCCCCEEECCHHH	27.91	UniProtKB CARBOHYD
163	O-linked_Glycosylation	TWLPFRTTVFSEEKL CCCCCCEEECCHHHH	18.46	UniProtKB CARBOHYD
185 (in isoform 2)	Ubiquitination	-	56.62	21906983
185 (in isoform 1)	Ubiquitination	-	56.62	21906983
185	Ubiquitination	EENWNAEKRSPTFHL HHCCCCHHCCCCEEC	56.62	2190698
226	N-linked_Glycosylation	ATPTPDQNASPYHTI ECCCCCCCCCCCCEE	50.17	UniProtKB CARBOHYD
247	Ubiquitination	LVDGLTDASSAFKVP EECCCCCCHHHCCCC	10.51	29967540
272	N-linked_Glycosylation	VDVFHFANDSRNMIY EEEEEECCCCCCEEE	47.01	15379548
298	Ubiquitination	QDPDELNKACSFSKP CCHHHHHHHHCCCCC	64.49	29967540
301	Phosphorylation	DELNKACSFSKPSNS HHHHHHHCCCCCCCC	37.10	24719451

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

Oops, there are no upstream regulatory protein records of ZP3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZP3_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 ZP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP2L_HUMAN	UBAP2L	physical	19945174
RT16_HUMAN	MRPS16	physical	19945174
SACA3_HUMAN	SPACA3	physical	19945174
OR2LD_HUMAN	OR2L13	physical	19945174
PCD17_HUMAN	PCDH17	physical	19945174
MILK1_HUMAN	MICALL1	physical	19945174

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

N-linked Glycosylation

"Mass spectrometry analysis of recombinant human ZP3 expressed inglycosylation-deficient CHO cells.";
Zhao M., Boja E.S., Hoodbhoy T., Nawrocki J., Kaufman J.B., Kresge N.,Ghirlando R., Shiloach J., Pannell L., Levine R.L., Fales H.M.,Dean J.;
Biochemistry 43:12090-12104(2004).
Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE FORMATION AT GLU-23,PROTEOLYTIC PROCESSING, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-125;ASN-147 AND ASN-272.
PubMed: 15379548